ID A2QBR6_ASPNC Unreviewed; 426 AA.
AC A2QBR6;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Contig An02c0010, genomic contig {ECO:0000313|EMBL:CAK96313.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:CAK96313.1};
GN ORFNames=An02g00990 {ECO:0000313|EMBL:CAK96313.1};
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:CAK96313.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK96313.1, 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).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; AM269996; CAK96313.1; -; Genomic_DNA.
DR RefSeq; XP_001399236.1; XM_001399199.1.
DR AlphaFoldDB; A2QBR6; -.
DR EnsemblFungi; CAK96313; CAK96313; An02g00990.
DR GeneID; 4978581; -.
DR KEGG; ang:An02g00990; -.
DR VEuPathDB; FungiDB:An02g00990; -.
DR HOGENOM; CLU_023257_6_0_1; -.
DR OrthoDB; 3684955at2759; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd05664; M20_Acy1-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:CAK96313.1};
KW Hydrolase {ECO:0000313|EMBL:CAK96313.1};
KW Protease {ECO:0000313|EMBL:CAK96313.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 208..303
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 426 AA; 46293 MW; 6F688DD40B5A5704 CRC64;
MTHSTTTISS LLNSSPVDLT PYEDLYKYFH AHPELSRQEK HTSEKLAAHL TQLGVFDIHT
HIGGYGLAGV FRNVTDEDKP HQTVLLRADM DALPVKELTN LPYASTITMH DTEGNDRPVM
HACGHDMHIT CLLAAAETLV KLRDAWSGTL IVLFQPDEER GGGAQAMVDD GLYSRIPVPD
VVLGQHVMRM RAGSVASRVG AIMAAADSMK ITVFGRGGHG SQPHQTVDPV LLAAHIVVRL
QSIVSREINP SDLAVLTVGS LQAGQTENII ADRAEIGVDF RSVRLEVREQ IIAGIKRIVQ
AECAASGSPA PPVFTPTRRF PPTVNDGVVA RRVAETFGEH FEDFDPDVPR TNIAEDFSTL
ATCRDIPSCF WLLGGVDQEV WDRAAAEGKI EEIPGNHSAL FAPVVQPTLR TGVDALCLAA
LTFLRK
//
