(data stored in ACNUC7421 zone)

SWISSPROT: A2Q8J7_ASPNC

ID   A2Q8J7_ASPNC            Unreviewed;      1068 AA.
AC   A2Q8J7;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 69.
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   Name=NAT10 {ECO:0000256|HAMAP-Rule:MF_03211};
GN   ORFNames=An01g04590 {ECO:0000313|EMBL:CAK36994.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK36994.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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 the tRNA-
CC       binding adapter protein TAN1 for full tRNA acetyltransferase activity
CC       but not for 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   -!- SUBUNIT: Interacts with TAN1. {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}.
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DR   EMBL; AM269963; CAK36994.1; -; Genomic_DNA.
DR   RefSeq; XP_001388886.1; XM_001388849.2.
DR   PaxDb; A2Q8J7; -.
DR   EnsemblFungi; CAK36994; CAK36994; An01g04590.
DR   GeneID; 4977260; -.
DR   KEGG; ang:ANI_1_586014; -.
DR   HOGENOM; HOG000210833; -.
DR   KO; K14521; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:1990883; F:rRNA cytidine N-acetyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0030515; F:snoRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0000049; F:tRNA binding; IEA:EnsemblFungi.
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;
DR   PRODOM; A2Q8J7.
DR   SWISS-2DPAGE; A2Q8J7.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03211};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03211};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03211};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_03211}.
FT   DOMAIN          108..202
FT                   /note="DUF1726"
FT                   /evidence="ECO:0000259|Pfam:PF08351"
FT   DOMAIN          283..499
FT                   /note="Helicase_RecD"
FT                   /evidence="ECO:0000259|Pfam:PF05127"
FT   DOMAIN          541..770
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13718"
FT   DOMAIN          779..1014
FT                   /note="tRNA_bind_2"
FT                   /evidence="ECO:0000259|Pfam:PF13725"
FT   NP_BIND         288..297
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT   REGION          642..644
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT   REGION          649..655
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT   REGION          1014..1068
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1057
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         481
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT   BINDING         743
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ   SEQUENCE   1068 AA;  119262 MW;  761C248A1319B285 CRC64;
     MPRKAIDSRI PALIRNGVQE KKRSFFVVVG DRAKDVIVHL HYIMSSVDVK QNKSVLWAYK
     KDLLGFTSHR KKREAKIKKE VKRGIREPNQ EDPFELFITL NQIRYVYYKE TEKILGNTYG
     MCVLQDFEAM TPNLLARTVE TVEGGGIVLL LLKGMNSLKQ LYTLSMDIHS RYRTEAHDDV
     TARFNERFIL SLGSCDSCLV VDDELNVLPI SGGKSVKPLP PPESIDDTNI GTKKELKEIK
     ESLAESQPIG SLVNLARTVD QAKALLTFAD AIAEKTLRST VALTAARGRG KSAALGVAIA
     AAVAHGYSNI FITSPSPENL KTLFEFVFKG FDALGYLDHV DYTILQSTNP DFNKAIVRVN
     IHRQHRQTIQ YIQPQDAHVL GQAELLVIDE AAAIPLPLVR KLMGPYLVFM ASTINGYEGT
     GRSLSLKLIQ QLREQSRGGV KVSGEDDIDV ADRATGKAAK NIDKSLAGRS LREITLSEPI
     RYAPGDSVEK WLNKVLCLDA TLPKSRMNTQ GTPHPSQCQL LQVNRDTLFS FHPVSEKFLQ
     QMMALYVASH YKNTPNDLQL MSDAPAHQLF VLVPPIDEEA TKLPEPLCVI QVALEGRISR
     QSVLNSLSRG QRAGGDLIPW LVSQQYQDED FAGLSGARIV RIATNPEYLS MGYGSRALEL
     LIDFYEGKFT SLSEDIPEPQ EEMVRVTDEE LTNSNLLDDN VKVRDIHTMP PLFGKLSERR
     PDALDYVGVS FGLTPSLHKF WKRSSFSPVY LRQTPNDLTG EHSCVMLRTL TSGSNDAAWL
     GAFSRDFHKR FSSLLSYQFR EFPSVLSLSI CESANSGAKL DPSISQSPLT KAELDAAFSP
     FDLKRLDSYA NNLLDYHVIL DMVPTIAEYY FSGRLSGKVS LSGVQQSILL AIGLQRKNLD
     TIEKELTLPS SQLLAMFLKI IRKVSTYFRN LIEGAVAETM PAEKAPSARV TTEAHDELPD
     ERFKPLETSL DDELREGGQE VNEELREKQR ALIDALPLDK YEINHGSAAW EEAEKQIRSG
     GASTVSVKTS KQTKRKKGES AREIYDQEID SKRQKIIKKG TEGKKKKH
//

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