NAT10_DROME
ID NAT10_DROME Reviewed; 1008 AA.
AC Q9W3C1; Q6NR51;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
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};
DE AltName: Full=Polycomb protein l(1)G0020;
DE AltName: Full=p110;
GN Name=l(1)G0020; ORFNames=CG1994;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11493925; DOI=10.1038/35088096;
RA Saurin A.J., Shao Z., Erdjument-Bromage H., Tempst P., Kingston R.E.;
RT "A Drosophila Polycomb group complex includes Zeste and dTAFII proteins.";
RL Nature 412:655-660(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-907, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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 (Probable). Polycomb group (PcG) protein. PcG
CC proteins act by forming multiprotein complexes, which are required to
CC maintain the transcriptionally repressive state of homeotic genes
CC throughout development. PcG proteins are not required to initiate
CC repression, but to maintain it during later stages of development. They
CC probably act via the methylation of histones, rendering chromatin
CC heritably changed in its expressibility (PubMed:11493925).
CC {ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000269|PubMed:11493925}.
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 -!- SUBUNIT: Component of the PRC1 complex (PSC, PC, PH and dRING1) in 0-12
CC hours Drosophila embryos. This complex is distinct from the Esc/E(z)
CC complex, which contains many other PcG proteins like Esc, E(z),
CC Su(z)12, HDAC1/Rpd3, Caf1-55 and probably Pho. The two complexes
CC however cooperate and interact together during the first 3 hours of
CC development to establish PcG silencing. {ECO:0000269|PubMed:11493925}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03211, ECO:0000269|PubMed:11493925}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03211}.
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DR EMBL; AE014298; AAF46410.2; -; Genomic_DNA.
DR EMBL; BT010228; AAQ23546.1; -; mRNA.
DR RefSeq; NP_572503.1; NM_132275.2.
DR AlphaFoldDB; Q9W3C1; -.
DR SMR; Q9W3C1; -.
DR BioGRID; 58270; 29.
DR DIP; DIP-21542N; -.
DR IntAct; Q9W3C1; 2.
DR STRING; 7227.FBpp0071217; -.
DR iPTMnet; Q9W3C1; -.
DR PaxDb; Q9W3C1; -.
DR PRIDE; Q9W3C1; -.
DR EnsemblMetazoa; FBtr0071280; FBpp0071217; FBgn0027330.
DR GeneID; 31811; -.
DR KEGG; dme:Dmel_CG1994; -.
DR FlyBase; FBgn0027330; l(1)G0020.
DR VEuPathDB; VectorBase:FBgn0027330; -.
DR eggNOG; KOG2036; Eukaryota.
DR GeneTree; ENSGT00390000009140; -.
DR InParanoid; Q9W3C1; -.
DR PhylomeDB; Q9W3C1; -.
DR SignaLink; Q9W3C1; -.
DR BioGRID-ORCS; 31811; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 31811; -.
DR PRO; PR:Q9W3C1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0027330; Expressed in eye disc (Drosophila) and 21 other tissues.
DR ExpressionAtlas; Q9W3C1; baseline and differential.
DR Genevisible; Q9W3C1; DM.
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:0016573; P:histone acetylation; IMP:FlyBase.
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; IPR016181; Acyl_CoA_acyltransferase.
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.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; ATP-binding; Developmental protein; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; rRNA processing;
KW Transcription; Transcription regulation; Transferase; tRNA processing.
FT CHAIN 1..1008
FT /note="RNA cytidine acetyltransferase"
FT /id="PRO_0000215886"
FT DOMAIN 531..713
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT REGION 950..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 282..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 601..603
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 608..614
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 700
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 28
FT /note="V -> I (in Ref. 3; AAQ23546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1008 AA; 112874 MW; 54F51677C5606CEB CRC64;
MVKKKIDNRI RVMIENGVKL GHRTMFIVIG DKARDQVPIL YDILTKSTVK ARPTVLWCYK
NKDEAISNHG KKRAKKIAVG KVDVNEADLF DSFRVATTIH GRYYSETHAV LGRTYGVCVL
QDFEALTPNL LARTVETVEG GGLIILLLKT LQSLKQLYTM SMDVHKRFRT EAHQTVTCRF
NERLILSLAD CKRCLVVNDD LTVLPLSSKT INVEPVNPAG AGRSPNEASL KELKESLLTV
QPAGALVNLC KTYDQANAVA QFIEALVDKQ LKPPMSLTAA RGRGKSAALG LSIAAAVAFG
YVNIYVTSPH PENLITLFEF VLKGFDALEY QEHADYTIIR STNADYKKAI IRINITRSSR
QTIQYIAPSD THLLNAADLL LIDEAAAIPL PLVKKMIGPY LVFMASTING YEGTGRSLSL
KLISQLQKDN NARPPLKLEE SIRYQENDDI EKWLINLLCL DASTVPSISS GCPTPDACEL
YYVDRDALFS YHKAAEAFLH RLVSIYVSSH YKNTPNDLQM MSDAPAHHLF CLLGPVQRMD
ALPEILVVIQ VALEGQISAQ SISDSLGRGK KAAGDLIPWN VAEQYGDRDF PKLCGVRIVR
VATHPNYQRM GYGKRAIQLL KDYYARKHTN LEDGPVASKD AGKGIEEVEE EELSLLKEQI
RPRSRIPTLL QRLHERVPEH VDYIGTSYGL TTELLKFWKN AGFVPVYLSQ KSNELTAEHS
CIMLHTPNAT PWLGLYYQDF RRRVLKLMGK TFREFETKLC LALLKNKSVD TEGSALKVLD
KPMLDVYFLP HDLQRLESYA RQQSEFRLII DLLTDIAQLY FQGRIDGLQL DLVQQGILLA
LGVQGKTVDA LGLELNMPGN QLLAKFFDAM KRCNQCFRSV LEEHIEGGML READLSKGEE
LQPLTLSLDK ELDQTAQKLS KQQRKELKRL KAEQLDEFQI KGTEEDWSKA LETNGTGGGS
GLLSVKSGVK RLDGPIETRE DGDLAAPLSK KKKKNNPKQR RSQGKSLI
