ID A0A1X0NTC6_9TRYP Unreviewed; 1061 AA. AC A0A1X0NTC6; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 17-JUN-2020, entry version 12. DE RecName: Full=RNA cytidine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03211}; DE EC=2.3.1.- {ECO:0000256|HAMAP-Rule:MF_03211}; DE AltName: Full=18S rRNA cytosine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03211}; GN ORFNames=TM35_000201320 {ECO:0000313|EMBL:ORC87723.1}; OS Trypanosoma theileri. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC87723.1, ECO:0000313|Proteomes:UP000192257}; RN [1] {ECO:0000313|EMBL:ORC87723.1, ECO:0000313|Proteomes:UP000192257} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edinburgh {ECO:0000313|EMBL:ORC87723.1}; RA Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P., RA Matthews J., Matthews K., Carrington M.; RT "An alternative strategy for trypanosome survival in the mammalian RT bloodstream revealed through genome and transcriptome analysis of the RT ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RNA cytidine acetyltransferase with specificity toward both CC 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine CC (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor CC rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the CC formation of ac4C in serine and leucine tRNAs. Requires a tRNA-binding CC adapter protein for full tRNA acetyltransferase activity but not for CC 18S rRNA acetylation. {ECO:0000256|HAMAP-Rule:MF_03211}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = ADP + an CC N(4)-acetylcytidine in 18S rRNA + CoA + H(+) + phosphate; CC Xref=Rhea:RHEA:51424, Rhea:RHEA-COMP:13575, Rhea:RHEA-COMP:13576, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03211}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a cytidine in tRNA + acetyl-CoA + ATP + H2O = ADP + an N(4)- CC acetylcytidine in tRNA + CoA + H(+) + phosphate; CC Xref=Rhea:RHEA:53876, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:13671, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03211}; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP- CC Rule:MF_03211}. CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03211}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ORC87723.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NBCO01000020; ORC87723.1; -; Genomic_DNA. DR OrthoDB; 296129at2759; -. DR Proteomes; UP000192257; Unassembled WGS sequence. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0000154; P:rRNA modification; IEA:UniProtKB-UniRule. DR GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-UniRule. DR HAMAP; MF_03211; RNA_acetyltr_Nat10; 1. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR007807; Helicase_dom. DR InterPro; IPR033688; NAT10. DR InterPro; IPR032672; TmcA/NAT10/Kre33. DR InterPro; IPR013562; TmcA_N. DR InterPro; IPR027992; tRNA_bind_dom. DR PANTHER; PTHR10925; PTHR10925; 1. DR Pfam; PF08351; DUF1726; 1. DR Pfam; PF13718; GNAT_acetyltr_2; 1. DR Pfam; PF05127; Helicase_RecD; 1. DR Pfam; PF13725; tRNA_bind_2; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03211}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03211}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03211}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03211}; KW Reference proteome {ECO:0000313|Proteomes:UP000192257}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_03211}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03211, ECO:0000313|EMBL:ORC87723.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03211}. FT DOMAIN 130..224 FT /note="DUF1726" FT /evidence="ECO:0000259|Pfam:PF08351" FT DOMAIN 312..517 FT /note="Helicase_RecD" FT /evidence="ECO:0000259|Pfam:PF05127" FT DOMAIN 558..788 FT /note="N-acetyltransferase" FT /evidence="ECO:0000259|Pfam:PF13718" FT DOMAIN 797..999 FT /note="tRNA_bind_2" FT /evidence="ECO:0000259|Pfam:PF13725" FT NP_BIND 318..327 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 658..660 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211" FT REGION 665..671 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211" FT REGION 691..721 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 971..1001 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1034..1061 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 259..279 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1036..1051 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 499 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211" FT BINDING 761 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211" SQ SEQUENCE 1061 AA; 117670 MW; 0124E3A7B9DB300C CRC64; MSSSASVVST AHSARGGSGG GVTIKRKVDD RIRNLIENAV HKKHRALILL VGDRGKDQIV NLHQMVSHAN HNAKVNMLWC MKKDPDFGST SKKQQEKRAR LEVKGGMSTE TTKEAFQTFL SQTQIRFCQY KETHKVLGQT FGMAVLQDFE AITPNTLART IETVKGGGVV VIMFRAMRSL KQLYTIAMDV HSRYRTEALR DVVPRFNERF LLSLVDCDTA LCVDDDLNVL PITAKMRAVE SMRTSNKSNY DADLALQGRQ KHEADLAALK ERLRASNEVG PLVSLCQTLD QGKTVLSLMQ TVVEKSLNTT CVVTAGRGRG KSAALGLAAA GALAQGYSNI FCTAPSPENL QTFFEFVVRG LQEQGYKERT DFEAMQSTNV EFSKCIVRIN LFREHRQTVQ YISPHDADKF AQAELAIIDE AAALPLPLVK QMLGPYLVFL SSTVSGYEGT GRSLSMKLIA DMRKQSGSIV GGSSSTSTAV STSDDRRFLR EITMTDPIRY GPNDPVESWL HKLLCLDATV RPLTVKSCPH PNKCELYYVN RDALFSYHPL AEQLLQTVVA MLVAAHYKNQ PNDLQLMSDA PGHHLFLLCS STVETNGELP DVFCVIHACE EGQVTSESIK SNLSRGVRPS GDLIPYTLSQ YYLEEGFAKL AGLRIVRIAT NPELQRAGYG SRALELLQQY YTGSISLQPA SSESLKTKEE TENNNNDNDD NDDTNSTSNV ITPRKRIPSL LTSLVERPYE VIDYLGVSFG VTTPLFNFWK RAGYEALYLR HAANELTGEH SCVMVRPIGF DLSLLRAEFH QRFIPLLSMP FRDLPTELAL SILNDLDVND PQKLAAATDH SQSSEHIVRV GGRLQCTLRE LQLIFNQNDM KRLRLNATTF VEGGLVLDLL PALAKLYFEA RLHRLPDGSE GVVLTHAQAA VLLAVGLQCQ TIEELSRQSA FAGVPLQQLR AFLQKAVARI VEHFTRLEKL KTPQEANGHS SVKNGEEGEE EDGEQEQTRE IYDKDGHVVG LSVEKKVQRV VNVDTTLLRD AKTAAIGTSK SESGTTGIQR AFKRSKKTRR S //