##gff-version 3
Q99JT2	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P289	
Q99JT2	UniProtKB	Chain	2	416	.	.	.	ID=PRO_0000086405;Note=Serine/threonine-protein kinase 26	
Q99JT2	UniProtKB	Domain	24	274	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q99JT2	UniProtKB	Region	296	343	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99JT2	UniProtKB	Compositional bias	327	341	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q99JT2	UniProtKB	Active site	144	144	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q99KH8,ECO:0000255|PROSITE-ProRule:PRU00159	
Q99JT2	UniProtKB	Binding site	30	38	.	.	.	Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q99KH8,ECO:0000255|PROSITE-ProRule:PRU00159	
Q99JT2	UniProtKB	Binding site	53	53	.	.	.	Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9P289,ECO:0000255|PROSITE-ProRule:PRU00159	
Q99JT2	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P289	
Q99JT2	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P289	
Q99JT2	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P289	
Q99JT2	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q99JT2	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P289	
Q99JT2	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P289	
Q99JT2	UniProtKB	Modified residue	309	309	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q99JT2	UniProtKB	Modified residue	325	325	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P289	
Q99JT2	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P289	
Q99JT2	UniProtKB	Modified residue	328	328	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P289