NAT10_CAEEL
ID NAT10_CAEEL Reviewed; 1043 AA.
AC O01757;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=RNA cytidine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03211};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03211};
DE AltName: Full=18S rRNA cytosine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03211};
GN Name=nath-10 {ECO:0000255|HAMAP-Rule:MF_03211}; ORFNames=F55A12.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_03211};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03211}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03211}.
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DR EMBL; FO080647; CCD65443.1; -; Genomic_DNA.
DR PIR; T15191; T15191.
DR RefSeq; NP_491574.1; NM_059173.4.
DR AlphaFoldDB; O01757; -.
DR SMR; O01757; -.
DR BioGRID; 37640; 2.
DR IntAct; O01757; 1.
DR STRING; 6239.F55A12.8; -.
DR EPD; O01757; -.
DR PaxDb; O01757; -.
DR PeptideAtlas; O01757; -.
DR EnsemblMetazoa; F55A12.8.1; F55A12.8.1; WBGene00018866.
DR GeneID; 172182; -.
DR KEGG; cel:CELE_F55A12.8; -.
DR UCSC; F55A12.8; c. elegans.
DR CTD; 172182; -.
DR WormBase; F55A12.8; CE11131; WBGene00018866; nath-10.
DR eggNOG; KOG2036; Eukaryota.
DR GeneTree; ENSGT00390000009140; -.
DR HOGENOM; CLU_004652_0_0_1; -.
DR InParanoid; O01757; -.
DR OMA; QDEEFAG; -.
DR OrthoDB; 296129at2759; -.
DR PhylomeDB; O01757; -.
DR PRO; PR:O01757; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00018866; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:1990883; F:rRNA cytidine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:1904812; P:rRNA acetylation involved in maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03211; RNA_acetyltr_Nat10; 1.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR007807; Helicase_dom.
DR InterPro; IPR033688; NAT10.
DR InterPro; IPR027417; P-loop_NTPase.
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; ATP-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; rRNA processing; Transferase; tRNA processing.
FT CHAIN 1..1043
FT /note="RNA cytidine acetyltransferase"
FT /id="PRO_0000215885"
FT DOMAIN 551..736
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT REGION 1020..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 622..624
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 629..635
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 723
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1043 AA; 116999 MW; D4AB383C9681A4FF CRC64;
MRTKLDGRIR TQIENGVASG HRSMFAVVGD KARDQVPILY HILSKSTVSA RPNVLWCYKK
ELSFSTHRAK KAKKMKKATT TISGSLPDAD PFDVFISSTQ IRYCYYNETE KILGNTFGVL
VLQDFEAMTP NLLARTIETI EGGGMVILLM QSVRSLRQLY TISMDVHNRY RTEAHNEITA
RFNERFILSL ASCSSVLVLD DQLRVLPISS HIENVEAIPA SQKKIQSESD AELASLKEAM
KETKPIGPLL SRARTACQAK ALLRFLDVIT EKQSNVTCSL TAGRGRGKSA AVGLSLAGAI
AFGYTNIFVT SPSPENLKTL FEFVVKGFDA LDYQEHTDYE LIQSANPEFK NCLVRINVFR
EHKQTIQYIS PTDVQKLGQC ELIVIDEAAA IPLPLVKELI SGPYISFLSS TINGYEGTGR
SLSLKLLQQL RQQSAGGEAK EGKSASNKGK TLHEMHMEES IRYKPGDKIE KWLNRLLCLD
ATNCQLKLEC GTPPPAACEL YIVNRDTLFS FHDASEAFLQ QVMAIFVSAH YKNSPNDLQM
LSDAPAHNLF VLMAPIDKSR KTIPEVLAVV QVCLEGRLDS DNIQNGLESG KRAAGDLLPW
TVSQQFMDKQ FGTLCGGRIV RVAVHPDYQS MGYGGRAVQL IEQYYLGLAT SLDEEEKAPA
PPSKTVIKQV KDGHTVELLE ERIEPRADLP PLLQRLDERK PERLDYLGVS FGLTVPLLKF
WKRNEFVPVY IRQNSNDITG EHTCIILKGL EHGGSDSDEE PSATWLPVYW REFRRRIVNL
LSFDFSSFPA QMALSLLQLK NKHVEKQMKR LVIERSELAI HLSNTDLRRM SQYGRNMVDS
HIITDILPIV AKLNFEQRLP QELKLAVTQS AILLARGLQH KHFEDISKEL DLPMNQIFAL
LTKAIRRIGD WFDEVCETAV RENLDKEAEA SAANKPTSSL PKAVPLANLE DELESAAKEI
RARHDRDRKA LLAELGNELQ KYEIIQDEKE LAEAYESVNM KYANKLVSVK SKRTAIQAAI
PDAKDPANKN AKKKKRFSSG GRR
