ID A2QXJ2_ASPNC Unreviewed; 466 AA.
AC A2QXJ2;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Contig An11c0300, genomic contig {ECO:0000313|EMBL:CAK97047.1};
DE EC=3.4.23.- {ECO:0000313|EMBL:CAK97047.1};
GN ORFNames=An11g09170 {ECO:0000313|EMBL:CAK97047.1};
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:CAK97047.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK97047.1, 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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; AM270247; CAK97047.1; -; Genomic_DNA.
DR RefSeq; XP_001394875.1; XM_001394838.1.
DR AlphaFoldDB; A2QXJ2; -.
DR EnsemblFungi; CAK97047; CAK97047; An11g09170.
DR GeneID; 4985133; -.
DR KEGG; ang:An11g09170; -.
DR VEuPathDB; FungiDB:An11g09170; -.
DR HOGENOM; CLU_032333_0_0_1; -.
DR OrthoDB; 2322499at2759; -.
DR Proteomes; UP000006706; Chromosome 7R.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAK97047.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..466
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002645488"
FT DOMAIN 63..377
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 466 AA; 50263 MW; F4DA642EB103B6E3 CRC64;
MTSSTLRLAV ALALSTCSSA LSSQRDDSLV VPFPFGNLED VHIAKRDSSK TVEAPLVIYG
DSYWMNASIG TPAQSLSFLL DLTRSRVEPA YTLDENYECS DDELCSEFGF YKPTDSSTYQ
HLTYTQRHDA GVDYSYLDTI TLGDHATDNV PLDMYLLSYI SYSSLGLSSV NTSFPYILVD
RGLTTSPSFS LIGDNGNTTT PSIIFGGINT SKFNGPLQAF SFADHSITNN PFVTVEADSL
QLTTNTNDNS TYPIPSSTPM MLRTEELITY LPNSTVQSLY TDLNITMDGV ISTSRFYGVL
PCARQETESH TISLAIGNMT FSVSWDELFV PWTRDGLCKF GIQAQDSDYK TRAELGVPFL
RRMYVAVDYN NQFVGVATLK DDDDQNGGED EIVEIGTGTA LPSAVGDWPA SVTAYTPAAS
TGTAAATLTF TTATSSGGGV VPTGLSELGR AFLVPGVLGM AVLQAV
//
