(data stored in SCRATCH zone)

SWISSPROT: C5DCS9_LACTC

ID   C5DCS9_LACTC            Unreviewed;      1055 AA.
AC   C5DCS9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 57.
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   OrderedLocusNames=KLTH0B05522g {ECO:0000313|EMBL:CAR21590.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21590.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21590.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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 the tRNA-binding adapter protein TAN1 for full
CC       tRNA 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   -!- 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.
CC       NAT10 subfamily. {ECO:0000256|HAMAP-Rule:MF_03211}.
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DR   EMBL; CU928166; CAR21590.1; -; Genomic_DNA.
DR   RefSeq; XP_002552028.1; XM_002551982.1.
DR   STRING; 381046.XP_002552028.1; -.
DR   EnsemblFungi; CAR21590; CAR21590; KLTH0B05522g.
DR   GeneID; 8290866; -.
DR   KEGG; lth:KLTH0B05522g; -.
DR   HOGENOM; HOG000210833; -.
DR   InParanoid; C5DCS9; -.
DR   KO; K14521; -.
DR   OMA; FWKRASF; -.
DR   OrthoDB; 296129at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
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;
DR   PRODOM; C5DCS9.
DR   SWISS-2DPAGE; C5DCS9.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03211};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
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       DUF1726. {ECO:0000259|Pfam:PF08351}.
FT   DOMAIN      281    491       Helicase_RecD. {ECO:0000259|Pfam:
FT                                PF05127}.
FT   DOMAIN      534    764       N-acetyltransferase. {ECO:0000259|Pfam:
FT                                PF13718}.
FT   DOMAIN      771   1007       tRNA_bind_2. {ECO:0000259|Pfam:PF13725}.
FT   NP_BIND     286    295       ATP. {ECO:0000256|HAMAP-Rule:MF_03211}.
FT   REGION      636    638       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03211}.
FT   REGION      643    649       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03211}.
FT   BINDING     473    473       ATP. {ECO:0000256|HAMAP-Rule:MF_03211}.
FT   BINDING     737    737       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_03211}.
SQ   SEQUENCE   1055 AA;  118282 MW;  20203EB0CD319287 CRC64;
     MAKKAIDSRI PSLIRNGAQT KQRSFFVIVG DKARNQLPNL HYLMMSADLK MNKSVLWAYK
     KKLLGFTSHR KKREAKIKKE IKRGTREVNE QDPFETFISN QNIRYVYYKE TEKILGNTYG
     MCILQDFEAL TPNLLARTVE TVEGGGIVVI LLKSMTSLKQ LYTMTMDIHS RYRTEAHSDV
     VARFNERFIL SLGSNENCLV VDDELNVLPI SGGKNVQPLP PKDEDEIPPR QQELIELKES
     LEDVQPAGSL VALSKTVNQA QAILNFIDAI SEKNLNSTVA LTAGRGRGKS AALGIAIAAA
     VSHGYSNIFV TSPSPENLKT LFEFIFKGFD ALGYQEHMDY DIIQSTNPSF NKAIVRVDIK
     KSHRQTIQYI VPNDSHVLGQ AELVVIDEAA AIPLPVVKNL LGPYLVFMAS TINGYEGTGR
     SLSLKLIQQL RDQANSSGRE TSETMVVSRD NKKQDFHASG RSLKEVVLDE PIRYAPGDPV
     EKWLNKLLCL DVTLIKNPRF AARGTPHPSE CNLFVVNRDT LFSYHPVSET FLEKMMALYV
     ASHYKNSPND LQLMSDAPAH QLFVLLPPIN PKDGGRIPDP LVVIQVALEG EISRDSVKSS
     LSRGQRAGGD LIPWLISQQF QDEEFPSLSG ARVVRVATNP EYSSMGYGSR AIELLRDYYE
     GKFADLNENS KPASHELKRV NDQELSKTNL LKDEVKLRDA KTLPPLLLKL SEQPPHFLHY
     LGVSYGLTSS LHKFWKKNKF VPVYLRQTAN DLTGEHTCVM LNVLEGRESH WLSEYANDFH
     KRFLSLLSYE FRKFSAVQAL NVIESVKKAN GLSGNAENKH AARPLTKEDI DQVLSPFDLK
     RLDSYANNLL DYHVIVDLLP LLSSLYFSGR MGSSVNLSSV QSAILLAVGL QRKSVDDVSK
     ELNLPFNQAI AMFAKIIRKF SIYFREVVSQ SIERSMPEAK DDNIAEMNGE EVTALDASSV
     MEKMDDDLEK AGTRALTAMQ EKQKELINSL NLDKYAIDDN AEEWAQSKKD LDKAAKKNGT
     VAVKSNKKRK TENAEDIFNA EMSAVKKSSK KKPKK
//

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