ID   PEPA_ASPFN              Reviewed;         404 AA.
AC   B8NLY9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Aspergillopepsin-1 {ECO:0000305};
DE            EC=3.4.23.18 {ECO:0000250|UniProtKB:Q12567};
DE   AltName: Full=Aspartic protease pepA;
DE   AltName: Full=Aspergillopepsin I;
DE   AltName: Full=Aspergillopeptidase A;
DE   Flags: Precursor;
GN   Name=pepA; ORFNames=AFLA_094450;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation of
CC       proteinaceous substrates. The scissile peptide bond is attacked by a
CC       nucleophilic water molecule activated by two aspartic residues in the
CC       active site. Shows a broad primary substrate specificity. Favors
CC       hydrophobic residues at the P1 and P1' positions, but also accepts a
CC       lysine residue in the P1 position, leading to the activation of
CC       trypsinogen and chymotrypsinogen A. {ECO:0000250|UniProtKB:Q12567}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity. Generally
CC         favors hydrophobic residues in P1 and P1', but also accepts Lys in
CC         P1, which leads to activation of trypsinogen. Does not clot milk.;
CC         EC=3.4.23.18; Evidence={ECO:0000250|UniProtKB:Q12567};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103}.
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DR   EMBL; EQ963480; EED49364.1; -; Genomic_DNA.
DR   RefSeq; XP_002381265.1; XM_002381224.1.
DR   AlphaFoldDB; B8NLY9; -.
DR   SMR; B8NLY9; -.
DR   MEROPS; A01.026; -.
DR   EnsemblFungi; EED49364; EED49364; AFLA_094450.
DR   VEuPathDB; FungiDB:AFLA_094450; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   OMA; YGSGNAK; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..77
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q12567"
FT                   /id="PRO_0000407041"
FT   CHAIN           78..404
FT                   /note="Aspergillopepsin-1"
FT                   /id="PRO_0000407042"
FT   DOMAIN          95..401
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        329..364
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   404 AA;  42313 MW;  BFC21C29EC0A24DF CRC64;
     MVILSKVAAV AVGLSTVASA LPTGPSHSPH ARRGFTINQI TRQTARVGPK TASFPAIYSR
     ALAKYGGTVP AHLKSAVASG HGTVVTSPEP NDIEYLTPVN IGGTTLNLDF DTGSADLWVF
     SEELPKSEQT GHDVYKPSGN ASKIAGASWD ISYGDGSSAS GDVYQDTVTV GGVTAQGQAV
     EAASKISDQF VQDKNNDGLL GLAFSSINTV KPKPQTTFFD TVKDQLDAPL FAVTLKYHAP
     GSYDFGFIDK SKFTGELAYA DVDDSQGFWQ FTADGYSVGK GDAQKAPITG IADTGTTLVM
     LDDEIVDAYY KQVQGAKNDA SAGGYVFPCE TELPEFTVVI GSYNAVIPGK HINYAPLQEG
     SSTCVGGIQS NSGLGLSILG DVFLKSQYVV FDSQGPRLGF AAQA