ID   A1YWA6_ASPNG            Unreviewed;       453 AA.
AC   A1YWA6;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-NOV-2023, entry version 69.
DE   SubName: Full=PEPAc {ECO:0000313|EMBL:ABM05949.1};
GN   Name=pepAc {ECO:0000313|EMBL:ABM05949.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:ABM05949.1};
RN   [1] {ECO:0000313|EMBL:ABM05949.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17977034; DOI=10.1016/j.fgb.2007.09.012;
RA   Wang Y., Xue W., Sims A.H., Zhao C., Wang A., Tang G., Qin J., Wang H.;
RT   "Isolation of four pepsin-like protease genes from Aspergillus niger and
RT   analysis of the effect of disruptions on heterologous laccase expression.";
RL   Fungal Genet. Biol. 45:17-27(2008).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF140758; ABM05949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1YWA6; -.
DR   MEROPS; A01.081; -.
DR   VEuPathDB; FungiDB:An12g03300; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1118349; -.
DR   VEuPathDB; FungiDB:ATCC64974_41680; -.
DR   VEuPathDB; FungiDB:M747DRAFT_266360; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
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:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..453
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002641638"
FT   DOMAIN          99..442
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   453 AA;  48095 MW;  7F096CBFF933675B CRC64;
     MYIPVGTLAT ASLLAGAALA APTPSPLKGR NIVRRSGSHT VYKPAAFAAP SHNKASSKYL
     ELSKTKSKGN VNPRSAAYVK RSTSSGSSSL ISLFEGEEFA TSITIGGDSF DVIVDTGSSD
     TWVVKTGFTC IDLDTGRETS ESSCDFGSTW TVESSFKEIE GEEFAIEYGD GEYLYGVMGN
     ETVALADITV DQTIGVVTEA AWEGDGTTSG LTGLAYPALT SAYSTTTDEQ IVYSNIITTM
     WEEGLIEPLF SLAIERDVSG AAGYLALGGL PPVDFVEDFT KTSILVTNIE GYSKAYDFYT
     INIDAVTLNG KSLTSAGGDD IQYIMQVDSG TTLNYYPTSI AEEINAAFSP AATYSDEEGA
     YIVDCDATPP THGITISGKT FYINPLDMIL DAGTDDEGNT ICISGIVDGG SDTSEDLYIL
     GDTFQKNVVT VFDIGATELR FAARENYTSN DTY
//