##gff-version 3 Q6DT37 UniProtKB Chain 1 1551 . . . ID=PRO_0000086397;Note=Serine/threonine-protein kinase MRCK gamma Q6DT37 UniProtKB Domain 71 337 . . . Note=Protein kinase;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000269|PubMed:15194684;Dbxref=PMID:15194684 Q6DT37 UniProtKB Domain 338 408 . . . Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618 Q6DT37 UniProtKB Domain 947 1066 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 Q6DT37 UniProtKB Domain 1092 1366 . . . Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795 Q6DT37 UniProtKB Domain 1437 1450 . . . Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057 Q6DT37 UniProtKB Zinc finger 878 927 . . . Note=Phorbol-ester/DAG-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 Q6DT37 UniProtKB Region 467 486 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q6DT37 UniProtKB Region 655 675 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q6DT37 UniProtKB Region 801 849 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q6DT37 UniProtKB Region 863 886 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q6DT37 UniProtKB Region 1442 1551 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q6DT37 UniProtKB Coiled coil 406 678 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q6DT37 UniProtKB Coiled coil 730 802 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q6DT37 UniProtKB Compositional bias 1460 1474 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q6DT37 UniProtKB Compositional bias 1510 1537 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q6DT37 UniProtKB Active site 195 195 . . . Note=Proton acceptor;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000255;evidence=ECO:0000250|UniProtKB:P54265,ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 Q6DT37 UniProtKB Binding site 77 85 . . . Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P54265,ECO:0000255|PROSITE-ProRule:PRU00159 Q6DT37 UniProtKB Binding site 100 100 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000269|PubMed:15194684;Dbxref=PMID:15194684 Q6DT37 UniProtKB Modified residue 216 216 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6DT37 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6DT37 UniProtKB Modified residue 234 234 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6DT37 UniProtKB Modified residue 1482 1482 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q6DT37 UniProtKB Natural variant 168 168 . . . ID=VAR_040840;Note=P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34454471,PMID:17344846 Q6DT37 UniProtKB Natural variant 280 280 . . . ID=VAR_040841;Note=In a glioblastoma multiforme sample%3B somatic mutation. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs770462360,PMID:17344846 Q6DT37 UniProtKB Natural variant 362 362 . . . ID=VAR_040842;Note=T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs55688429,PMID:17344846 Q6DT37 UniProtKB Natural variant 537 537 . . . ID=VAR_040843;Note=A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34241745,PMID:17344846 Q6DT37 UniProtKB Natural variant 1135 1135 . . . ID=VAR_057105;Note=Q->R;Dbxref=dbSNP:rs3741395 Q6DT37 UniProtKB Sequence conflict 628 628 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305