ID A2QZB2_ASPNC Unreviewed; 313 AA.
AC A2QZB2;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Contig An12c0120, genomic contig {ECO:0000313|EMBL:CAK46197.1};
DE EC=3.1.1.- {ECO:0000313|EMBL:CAK46197.1};
GN ORFNames=An12g04280 {ECO:0000313|EMBL:CAK46197.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK46197.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK46197.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {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; AM270268; CAK46197.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QZB2; -.
DR EnsemblFungi; CAK46197; CAK46197; An12g04280.
DR VEuPathDB; FungiDB:An12g04280; -.
DR HOGENOM; CLU_042179_3_0_1; -.
DR Proteomes; UP000006706; Chromosome 3L.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF29; LIPASE_THIOESTERASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_8G02590); 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CAK46197.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..313
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002644454"
FT DOMAIN 104..303
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
SQ SEQUENCE 313 AA; 34371 MW; A24B08EE357C9D82 CRC64;
MELLAILGLL WAISKASSWT ALQAPVRGPR GGTAATKHIM AMAVRTFFET VSIDQFRYAY
SPDTSARLLE TWARCTHTTL KKVKLPDGTT AFWLGNPDAE RLLLHLPGGA YCLPALPSHI
DYSTSILKGL GQAGIDAGML FLPYELTPTA QYPHQMKQAV ALLQYVIEDL GKRPSDIVLL
GDSAGAHLIL SVLSHLAHPH PHIPPLLLPE NLAGALLLSP WMGESRTDYD SCRRNASRDL
VSLKLLIHWA DMFLGDTEPD SYNQPAGAPG GWWRDLPVEE IFIGVGGHEI LYDSIIKTAR
KIKCYGLWDN ASD
//
