##gff-version 3 P27636 UniProtKB Chain 1 974 . . . ID=PRO_0000085717;Note=Cell division control protein 15 P27636 UniProtKB Domain 25 272 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P27636 UniProtKB Region 360 702 . . . Note=Self association domain P27636 UniProtKB Region 554 592 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P27636 UniProtKB Region 751 974 . . . Note=Auto-inhibitory domain P27636 UniProtKB Region 941 974 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P27636 UniProtKB Compositional bias 960 974 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P27636 UniProtKB Active site 146 146 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P27636 UniProtKB Binding site 31 39 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P27636 UniProtKB Binding site 54 54 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P27636 UniProtKB Modified residue 561 561 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22031224;Dbxref=PMID:22031224 P27636 UniProtKB Modified residue 567 567 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22031224,ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198,PMID:22031224 P27636 UniProtKB Modified residue 870 870 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22031224;Dbxref=PMID:22031224 P27636 UniProtKB Sequence conflict 316 316 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P27636 UniProtKB Sequence conflict 321 321 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 P27636 UniProtKB Sequence conflict 900 902 . . . Note=KDV->NGC;Ontology_term=ECO:0000305;evidence=ECO:0000305