NAT10_DICDI
ID NAT10_DICDI Reviewed; 1057 AA.
AC Q55EJ3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=nat10 {ECO:0000312|dictyBase:DDB_G0268868};
GN ORFNames=DDB_G0268868 {ECO:0000312|dictyBase:DDB_G0268868};
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000004; EAL73023.1; -; Genomic_DNA.
DR RefSeq; XP_647027.1; XM_641935.1.
DR AlphaFoldDB; Q55EJ3; -.
DR SMR; Q55EJ3; -.
DR STRING; 44689.DDB0234062; -.
DR PaxDb; Q55EJ3; -.
DR EnsemblProtists; EAL73023; EAL73023; DDB_G0268868.
DR GeneID; 8616722; -.
DR KEGG; ddi:DDB_G0268868; -.
DR dictyBase; DDB_G0268868; nat10.
DR eggNOG; KOG2036; Eukaryota.
DR HOGENOM; CLU_004652_0_0_1; -.
DR InParanoid; Q55EJ3; -.
DR OMA; QDEEFAG; -.
DR PhylomeDB; Q55EJ3; -.
DR PRO; PR:Q55EJ3; -.
DR Proteomes; UP000002195; Chromosome 1.
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; 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 3: Inferred from homology;
KW Acyltransferase; ATP-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; rRNA processing; Transferase; tRNA processing.
FT CHAIN 1..1057
FT /note="RNA cytidine acetyltransferase"
FT /id="PRO_0000327396"
FT DOMAIN 549..682
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT REGION 654..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 284..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 621..623
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 628..634
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 730
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1057 AA; 120004 MW; 9FB23EAE077E566C CRC64;
MVRKKVDTRI RTLIENGVAT NHRSFFVIVG DNGKDQVPNL HYILSKSIVK ARPSVLWCYK
EDLGFSKHKK KKMKLKEKSK SSGIDSVNQE DPFDVFISTT NIRYSYYSES HKILGNTFGM
LVLQDFEAIT PNLLARTIET VEGGGLIVLL LKTMDSLKQL YTMTMDVHTR FRSENSKGEV
VCRFNERFLL SLGKSEQCLV MDDELNILPI SSQSRSIEAK QQILETPEQV ELREFKQQVK
DTDIAGALIE NTKTMDQATA LLTFIDSISE KTLRSTVTLT AGRGRGKSAA LGLAISAAVA
FGYSNIFVSS PTPENLNTLF QFVFKGFDSM EYVEHVDYEL VKSTNPEFHD AIIRVNIFRS
HRQTIQYIQP QDYQKLGQAE LVVIDEAAAI PLPLVKNLLG PYLVFMSSTI NGYEGTGRSL
SLKLIKQLRE QSTVVSNSSN KALNSITGRM LREIELNEPI RYSARDPIER WLNELLCLDS
TIAKSSPTGC PHPSACQLYY VNRDTLFSYH KASEAFLQKM VGLFVSSHYK NSPNDLLLMS
DAPDHHLFVL LGPIDENNTT GLPEILCAVQ VSLEGEIAKE SILNSIKRGY QASGDLIPWT
LTQQYQDEDF PRLSGVRIVR IATHPDYQKM GYGSKALELL TQYYQGEITN LDEVNQEEEE
EDEEKVDQNK GSSKISTVKK DNASLLTEVI RPKSNIPPLL FKLSERKPEK LHYMGVSYGL
TQQLYQFWSK SKYLPVYLRL TSNDITGEHT CIMLRELNNE QNNTICKDGW LQSFHQDFKK
RFINLLGYEF RNFNSSIALN ILYEKKVNNT VAVASSTTKN ELTQNEMELL FSSYDLKRLE
SYSNNIVDYH VVIDLLPSLS KLYFTNKLKI EDISLIQSAI LLALGLQHKT VDNLIGELNL
ASNQVLSLFN QTMRKINTEL KQKQEKFIQD SMPKLSIVAP RTGQFKSFKG DIKETDMIPL
AEDMESELEK GAEEVVNKLK HQLENDSSLS KYLVKGNDED WSKALKPGSI PNSITIKRKS
DENEETDKKE NNKKSKTKNN NNNNNNNKKV NNQKSKK
