##gff-version 3
P00956	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6390679,ECO:0000269|PubMed:7929087;Dbxref=PMID:6390679,PMID:7929087	
P00956	UniProtKB	Chain	2	938	.	.	.	ID=PRO_0000098384;Note=Isoleucine--tRNA ligase	
P00956	UniProtKB	Motif	58	68	.	.	.	Note='HIGH' region	
P00956	UniProtKB	Motif	602	606	.	.	.	Note='KMSKS' region	
P00956	UniProtKB	Binding site	561	561	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P00956	UniProtKB	Binding site	602	602	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19557155;Dbxref=PMID:19557155	
P00956	UniProtKB	Binding site	605	605	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19557155;Dbxref=PMID:19557155	
P00956	UniProtKB	Binding site	901	901	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P00956	UniProtKB	Binding site	904	904	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P00956	UniProtKB	Binding site	921	921	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P00956	UniProtKB	Binding site	924	924	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P00956	UniProtKB	Modified residue	183	183	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18723842;Dbxref=PMID:18723842	
P00956	UniProtKB	Natural variant	300	301	.	.	.	Note=In strain: EM20031%2C MRE-600%3B AA sequence. EL->DV;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19557155,ECO:0000269|PubMed:6390679;Dbxref=PMID:19557155,PMID:6390679	
P00956	UniProtKB	Natural variant	587	587	.	.	.	Note=In strain: MRE-600%3B AA sequence. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6390679;Dbxref=PMID:6390679	
P00956	UniProtKB	Natural variant	594	594	.	.	.	Note=In strain: PS102. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7929087;Dbxref=PMID:7929087	
P00956	UniProtKB	Natural variant	637	637	.	.	.	Note=In strain: MRE-600%3B AA sequence. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6390679;Dbxref=PMID:6390679	
P00956	UniProtKB	Natural variant	724	724	.	.	.	Note=In strain: EM20031%3B AA sequence. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19557155;Dbxref=PMID:19557155	
P00956	UniProtKB	Natural variant	738	738	.	.	.	Note=In strain: EM20031%2C MRE-600%3B AA sequence. A->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19557155,ECO:0000269|PubMed:6390679;Dbxref=PMID:19557155,PMID:6390679	
P00956	UniProtKB	Natural variant	740	743	.	.	.	Note=In strain: EM20031%3B AA sequence. ADSV->RTVW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19557155;Dbxref=PMID:19557155	
P00956	UniProtKB	Natural variant	787	787	.	.	.	Note=In strain: MRE-600%3B AA sequence. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6390679;Dbxref=PMID:6390679	
P00956	UniProtKB	Natural variant	830	830	.	.	.	Note=In strain: MRE-600%3B AA sequence. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6390679;Dbxref=PMID:6390679	
P00956	UniProtKB	Mutagenesis	94	94	.	.	.	Note=6000-fold increase in Km for isoleucine and 4-fold increase in Km for ATP%2C with no effect on activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3282306;Dbxref=PMID:3282306	
P00956	UniProtKB	Mutagenesis	97	97	.	.	.	Note=No effect on activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3282306;Dbxref=PMID:3282306	
P00956	UniProtKB	Mutagenesis	102	102	.	.	.	Note=No significant effect on activity. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3282306;Dbxref=PMID:3282306	
P00956	UniProtKB	Mutagenesis	183	183	.	.	.	Note=Abolishes translocation from the aminoacylation site to the editing site%2C without effect on aminoacylation activity and posttransfer editing%3B when associated with A-421. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12515858;Dbxref=PMID:12515858	
P00956	UniProtKB	Mutagenesis	241	241	.	.	.	Note=Nearly the same editing activity as the wild-type. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9554847;Dbxref=PMID:9554847	
P00956	UniProtKB	Mutagenesis	242	242	.	.	.	Note=Abolishes editing activity against valine%2C with little change in aminoacylation activity%3B when associated with A-250. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10889024;Dbxref=PMID:10889024	
P00956	UniProtKB	Mutagenesis	242	242	.	.	.	Note=Abolishes editing activity against valine%2C with little change in aminoacylation activity. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10889024;Dbxref=PMID:10889024	
P00956	UniProtKB	Mutagenesis	243	243	.	.	.	Note=Abolishes editing activity against valine%2C with little change in aminoacylation activity. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11864608,ECO:0000269|PubMed:9554847;Dbxref=PMID:11864608,PMID:9554847	
P00956	UniProtKB	Mutagenesis	243	243	.	.	.	Note=Abolishes pretransfer editing. T->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11864608,ECO:0000269|PubMed:9554847;Dbxref=PMID:11864608,PMID:9554847	
P00956	UniProtKB	Mutagenesis	246	246	.	.	.	Note=Nearly the same editing activity as the wild-type. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9554847;Dbxref=PMID:9554847	
P00956	UniProtKB	Mutagenesis	250	250	.	.	.	Note=Abolishes editing activity against valine%2C with little change in aminoacylation activity. N->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10889024,ECO:0000269|PubMed:9554847;Dbxref=PMID:10889024,PMID:9554847	
P00956	UniProtKB	Mutagenesis	333	333	.	.	.	Note=Alters the specificity for hydrolysis of the aminoacyl tRNA ester%2C with no effect on pretransfer editing. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864608;Dbxref=PMID:11864608	
P00956	UniProtKB	Mutagenesis	342	342	.	.	.	Note=Strong decrease in total editing and deacylation activities. Severely deficient in translocation from the aminoacylation site to the editing site. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11782529;Dbxref=PMID:11782529	
P00956	UniProtKB	Mutagenesis	342	342	.	.	.	Note=Reduces 2- to 3-fold the total editing activity and 2-fold the deacylation activity. Moderately reduces translocation from the aminoacylation site to the editing site. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11782529;Dbxref=PMID:11782529	
P00956	UniProtKB	Mutagenesis	421	421	.	.	.	Note=Abolishes translocation from the aminoacylation site to the editing site%2C without effect on aminoacylation activity and posttransfer editing%3B when associated with A-183. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12515858;Dbxref=PMID:12515858