##gff-version 3
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	Region	552	668	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P40494	UniProtKB	Region	733	761	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P40494	UniProtKB	Region	743	756	.	.	.	Note=Interaction with SH3 domain of ABP1	
P40494	UniProtKB	Compositional bias	552	592	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P40494	UniProtKB	Compositional bias	593	616	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P40494	UniProtKB	Compositional bias	624	642	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P40494	UniProtKB	Compositional bias	643	668	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P40494	UniProtKB	Compositional bias	733	752	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
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	28	36	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P40494	UniProtKB	Binding site	56	56	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P40494	UniProtKB	Modified residue	402	402	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18407956,ECO:0007744|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
P40494	UniProtKB	Modified residue	428	428	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198	
P40494	UniProtKB	Modified residue	484	484	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18407956,ECO:0007744|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198	
P40494	UniProtKB	Modified residue	553	553	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198	
P40494	UniProtKB	Modified residue	556	556	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|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	Mutagenesis	158	158	.	.	.	Note=Loss of catalytic activity. D->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11739778,ECO:0000269|PubMed:13679512,ECO:0000269|PubMed:9885245;Dbxref=PMID:11739778,PMID:13679512,PMID:9885245	
P40494	UniProtKB	Sequence conflict	786	786	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305