(data stored in SCRATCH zone)

SWISSPROT: B6H1Z4_PENRW

ID   B6H1Z4_PENRW            Unreviewed;      1035 AA.
AC   B6H1Z4;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, 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   ORFNames=Pc13g03430 {ECO:0000313|EMBL:CAP91412.1}, PCH_Pc13g03430
GN   {ECO:0000313|EMBL:CAP91412.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91412.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91412.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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: A cytidine in 18S rRNA + ATP + acetyl-CoA +
CC       H(2)O = an N(4)-acetylcytidine in 18S rRNA + ADP + phosphate +
CC       CoA. {ECO:0000256|HAMAP-Rule:MF_03211}.
CC   -!- CATALYTIC ACTIVITY: A cytidine in tRNA + ATP + acetyl-CoA + H(2)O
CC       = an N(4)-acetylcytidine in tRNA + ADP + phosphate + CoA.
CC       {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; AM920428; CAP91412.1; -; Genomic_DNA.
DR   RefSeq; XP_002558780.1; XM_002558734.1.
DR   STRING; 500485.XP_002558780.1; -.
DR   EnsemblFungi; CAP91412; CAP91412; PCH_Pc13g03430.
DR   GeneID; 8313443; -.
DR   KEGG; pcs:Pc13g03430; -.
DR   eggNOG; KOG2036; Eukaryota.
DR   eggNOG; COG1444; LUCA.
DR   HOGENOM; HOG000210833; -.
DR   KO; K14521; -.
DR   OMA; RLLKFWK; -.
DR   OrthoDB; EOG092C0F0X; -.
DR   BioCyc; PCHR:PC13G03430-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000154; P:rRNA modification; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-HAMAP.
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; B6H1Z4.
DR   SWISS-2DPAGE; B6H1Z4.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03211};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
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      283    496       Helicase_RecD. {ECO:0000259|Pfam:
FT                                PF05127}.
FT   DOMAIN      538    767       N-acetyltransferase. {ECO:0000259|Pfam:
FT                                PF13718}.
FT   DOMAIN      776    989       tRNA_bind_2. {ECO:0000259|Pfam:PF13725}.
FT   NP_BIND     288    297       ATP. {ECO:0000256|HAMAP-Rule:MF_03211}.
FT   REGION      639    641       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03211}.
FT   REGION      646    652       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03211}.
FT   COILED      659    686       {ECO:0000256|SAM:Coils}.
FT   BINDING     478    478       ATP. {ECO:0000256|HAMAP-Rule:MF_03211}.
FT   BINDING     740    740       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_03211}.
SQ   SEQUENCE   1035 AA;  115693 MW;  116E9183429B62CA CRC64;
     MPRKAIDSRI PALIRNGVQE KKRSFFVVVG DHAKDVIVHL HYIMSSVDVK QNKSVLWAYK
     KDLLGFTSHR KKREMKIKKE VKRGIREPNQ EDPFELFITL NQIRYVYYKE TEKILGNTYG
     MCVLQDFEAM TPNLLARTVE TVEGGGLVIL LLKSMTSLKQ LYTMSMDIHS RYRTEAHDDV
     VARFNERFIL SLGSCDSCLV VDDELNVLPI SGGKSVKPLP APETTDESAS GTKKELKEIK
     ESLADSKPVG PLLSLARTVD QAKALLTFVD AIAEKTLKST VTLTAGRGRG KSAALGVAIA
     AAVAHGYSNI FITSPSPENL KTLFEFIFKG FDALGYLDHV DYTILQSTNP DFNKAVVRVN
     IHRNHRQTIQ YIQPQDAQVL GQAELLVIDE AAAIPLPLVR KLMGPYLVFM SSTINGYEGT
     GRSLSLKLIQ QLREQSRTGV KTDDTDIADR STGKSAKGAD KNLSGRTLRE ITLSEPIRYA
     PGDSVEKWLN KVLCLDATLP KSHMNTQGCP HPSQCQLLQV NRDTLFSFHP VSEKFLQQMM
     ALYVASHYKN TPNDLQLMSD APAHQLYVLV PPIDEGATKL PEPLCVIQVA LEGRISRQSV
     LNSLSRGQRA GGDLIPWLVS QQFQDENFAS LSGARIVRIA TNPEYVGMGY GSRAMQLLVD
     FFEGKFTNLE EENIAAEEQM VRVTDEELAS SSLLDDNVHV RDIRSMPPLF GKLTERRPDV
     LDYVGVSYGL TPSLHKFWKR GSFVPVYLRQ TPNELTGEHS CVMVRTLSTG EADDAWLSAY
     ARDFHKRFLS LMSYQFGQFP SVLSLSICEA ANSGAKKDPT FKPRTLQKAD LDAAFSPFDL
     KRLDSYANNL LDYHVILDLV PALSDYYFAN RLDGKVSLSG VQQSILLAIG LQHKSLDDLE
     KELNLPSSQL LAMFLKIVRK VSTHFRNLIE NEIEQSLPAQ KVRVETSAAH DDEPEVNLQP
     LPISLEDELR EGSKKIDEEM LAKQRALSAA NPDGPDGSKS SKRKKIETAR DIYDKEIDSK
     RQKMIKKGTE GRKKR
//

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