##gff-version 3
Q7TSE6	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2H1	
Q7TSE6	UniProtKB	Chain	2	464	.	.	.	ID=PRO_0000086721;Note=Serine/threonine-protein kinase 38-like	
Q7TSE6	UniProtKB	Domain	90	383	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q7TSE6	UniProtKB	Domain	384	453	.	.	.	Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618	
Q7TSE6	UniProtKB	Region	64	89	.	.	.	Note=S100B binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q7TSE6	UniProtKB	Active site	213	213	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
Q7TSE6	UniProtKB	Binding site	96	104	.	.	.	Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:O95835,ECO:0000255|PROSITE-ProRule:PRU00159	
Q7TSE6	UniProtKB	Binding site	119	119	.	.	.	Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9Y2H1,ECO:0000255|PROSITE-ProRule:PRU00159	
Q7TSE6	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2H1	
Q7TSE6	UniProtKB	Modified residue	75	75	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2H1	
Q7TSE6	UniProtKB	Modified residue	282	282	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2H1	
Q7TSE6	UniProtKB	Modified residue	442	442	.	.	.	Note=Phosphothreonine%3B by STK24/MST3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2H1	
Q7TSE6	UniProtKB	Alternative sequence	423	423	.	.	.	ID=VSP_012334;Note=In isoform 2. V->VAFFLFLV;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
Q7TSE6	UniProtKB	Sequence conflict	97	97	.	.	.	Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305