##gff-version 3 Q9H0A0 UniProtKB Chain 1 1025 . . . ID=PRO_0000215883;Note=RNA cytidine acetyltransferase Q9H0A0 UniProtKB Domain 558 753 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03211 Q9H0A0 UniProtKB Region 702 1025 . . . Note=Required for localization to the nucleolus and midbody;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19303003;Dbxref=PMID:19303003 Q9H0A0 UniProtKB Region 990 1025 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H0A0 UniProtKB Compositional bias 990 1015 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H0A0 UniProtKB Binding site 287 296 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03211 Q9H0A0 UniProtKB Binding site 470 470 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03211 Q9H0A0 UniProtKB Binding site 629 631 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03211 Q9H0A0 UniProtKB Binding site 636 642 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03211 Q9H0A0 UniProtKB Binding site 725 725 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03211 Q9H0A0 UniProtKB Modified residue 426 426 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:27993683,ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861,PMID:27993683 Q9H0A0 UniProtKB Modified residue 716 716 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9H0A0 UniProtKB Modified residue 934 934 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q9H0A0 UniProtKB Modified residue 984 984 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q9H0A0 UniProtKB Modified residue 987 987 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q9H0A0 UniProtKB Alternative sequence 1 72 . . . ID=VSP_054018;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9H0A0 UniProtKB Natural variant 461 461 . . . ID=VAR_059858;Note=Y->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:11214970,ECO:0000269|PubMed:11230166,ECO:0000269|PubMed:14592445,ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0007744|PubMed:21269460;Dbxref=dbSNP:rs2957516,PMID:11214970,PMID:11230166,PMID:14592445,PMID:14702039,PMID:15489334,PMID:21269460 Q9H0A0 UniProtKB Natural variant 983 983 . . . ID=VAR_061894;Note=A->T;Dbxref=dbSNP:rs36006049 Q9H0A0 UniProtKB Mutagenesis 426 426 . . . Note=Abolished acetylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27993683;Dbxref=PMID:27993683 Q9H0A0 UniProtKB Mutagenesis 641 641 . . . Note=Abolished acetyltransferase activity%2C probably caused by impaired acetyl-CoA binding. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24786082;Dbxref=PMID:24786082 Q9H0A0 UniProtKB Sequence conflict 26 26 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H0A0 UniProtKB Sequence conflict 162 162 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H0A0 UniProtKB Sequence conflict 315 315 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H0A0 UniProtKB Sequence conflict 405 405 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H0A0 UniProtKB Sequence conflict 879 879 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H0A0 UniProtKB Sequence conflict 971 971 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H0A0 UniProtKB Helix 893 906 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VLA