(data stored in ACNUC7421 zone)

SWISSPROT: A2Q8P1_ASPNC

ID   A2Q8P1_ASPNC            Unreviewed;       198 AA.
AC   A2Q8P1;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 73.
DE   SubName: Full=Aspergillus niger contig An01c0170, genomic contig {ECO:0000313|EMBL:CAK37038.1};
DE            EC=3.6.1.23 {ECO:0000313|EMBL:CAK37038.1};
GN   ORFNames=An01g05040 {ECO:0000313|EMBL:CAK37038.1};
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:CAK37038.1, 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).
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DR   EMBL; AM269964; CAK37038.1; -; Genomic_DNA.
DR   RefSeq; XP_001388930.1; XM_001388893.1.
DR   PaxDb; A2Q8P1; -.
DR   EnsemblFungi; CAK37038; CAK37038; An01g05040.
DR   GeneID; 4978165; -.
DR   KEGG; ang:ANI_1_640014; -.
DR   HOGENOM; HOG000028966; -.
DR   KO; K01520; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR008181; dUTPase_1.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   PANTHER; PTHR11241; PTHR11241; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR00576; dut; 1.
PE   4: Predicted;
DR   PRODOM; A2Q8P1.
DR   SWISS-2DPAGE; A2Q8P1.
KW   Hydrolase {ECO:0000313|EMBL:CAK37038.1}.
FT   DOMAIN          71..197
FT                   /note="dUTPase"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..62
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  20821 MW;  5F9C01B5A940E9B2 CRC64;
     MTKETTPPPP TTTTTEPTTN TTHEPPSLPA SPLAKRTKPN TTEQSTEPST MGSTSTPLPP
     LQVKKLTPTG RAPTRGSAFA AGYDMYSAKE TVIPAKGKAL VDTGIAIAVP EGTYGRIAPR
     SGLASKHFID TGAGVIDADY RGEVKVLLFN HSDVDFEVKE GDRVAQLVLE RIYTPEVVVV
     EELAESVRGA GGFGSTGV
//

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