##gff-version 3
P17714	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P17714	UniProtKB	Chain	2	561	.	.	.	ID=PRO_0000056911;Note=Asparagine synthetase [glutamine-hydrolyzing]	
P17714	UniProtKB	Domain	2	191	.	.	.	Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609	
P17714	UniProtKB	Domain	213	536	.	.	.	Note=Asparagine synthetase	
P17714	UniProtKB	Active site	2	2	.	.	.	Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P17714	UniProtKB	Binding site	49	53	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P17714	UniProtKB	Binding site	75	77	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P17714	UniProtKB	Binding site	97	97	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P17714	UniProtKB	Binding site	256	256	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P17714	UniProtKB	Binding site	288	288	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P17714	UniProtKB	Binding site	363	364	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P17714	UniProtKB	Site	365	365	.	.	.	Note=Important for beta-aspartyl-AMP intermediate formation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P17714	UniProtKB	Modified residue	385	385	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08243	
P17714	UniProtKB	Modified residue	545	545	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08243	
P17714	UniProtKB	Modified residue	557	557	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08243	
P17714	UniProtKB	Mutagenesis	414	414	.	.	.	Note=In ts11%3B temperature-sensitive. Blocked in the G1 phase of the cell cycle at the non-permissive temperature (39.5 degrees Celsius). Heat labile. L->F