ID A0A1X0NTC6_9TRYP Unreviewed; 1061 AA. AC A0A1X0NTC6; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 31-JUL-2019, entry version 10. 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; Euglenozoa; Kinetoplastida; 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., RA Voorheis P., 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 CC both 18S rRNA and tRNAs. Catalyzes the formation of N(4)- CC acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar CC cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA CC synthesis. Catalyzes the formation of ac4C in serine and leucine CC tRNAs. Requires a tRNA-binding adapter protein for full tRNA CC acetyltransferase activity but not for 18S rRNA acetylation. CC {ECO:0000256|HAMAP-Rule:MF_03211}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = ADP + CC an N(4)-acetylcytidine in 18S rRNA + CoA + H(+) + phosphate; CC Xref=Rhea:RHEA:51424, Rhea:RHEA-COMP:13575, Rhea:RHEA- CC COMP:13576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|HAMAP-Rule:MF_03211}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a cytidine in tRNA + acetyl-CoA + ATP + H2O = ADP + an CC N(4)-acetylcytidine in tRNA + CoA + H(+) + phosphate; CC Xref=Rhea:RHEA:53876, Rhea:RHEA-COMP:13670, Rhea:RHEA- CC COMP:13671, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, CC ChEBI:CHEBI:456216; 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. CC NAT10 subfamily. {ECO:0000256|HAMAP-Rule:MF_03211}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Complete proteome {ECO:0000313|Proteomes:UP000192257}; 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, KW ECO:0000313|EMBL:ORC87723.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03211}. FT DOMAIN 130 224 DUF1726. {ECO:0000259|Pfam:PF08351}. FT DOMAIN 312 517 Helicase_RecD. {ECO:0000259|Pfam: FT PF05127}. FT DOMAIN 558 788 N-acetyltransferase. {ECO:0000259|Pfam: FT PF13718}. FT DOMAIN 797 999 tRNA_bind_2. {ECO:0000259|Pfam:PF13725}. FT NP_BIND 318 327 ATP. {ECO:0000256|HAMAP-Rule:MF_03211}. FT REGION 1 24 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 658 660 Acetyl-CoA binding. {ECO:0000256|HAMAP- FT Rule:MF_03211}. FT REGION 665 671 Acetyl-CoA binding. {ECO:0000256|HAMAP- FT Rule:MF_03211}. FT REGION 691 721 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 971 1001 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 1034 1061 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COILED 259 279 {ECO:0000256|SAM:Coils}. FT COMPBIAS 1036 1051 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT BINDING 499 499 ATP. {ECO:0000256|HAMAP-Rule:MF_03211}. FT BINDING 761 761 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT 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 //