ID   PEPA_ASPFC              Reviewed;         395 AA.
AC   B0Y1V8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=AFUB_061010;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499597; EDP52067.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y1V8; -.
DR   SMR; B0Y1V8; -.
DR   Allergome; 63; Asp f 10.
DR   MEROPS; A01.026; -.
DR   EnsemblFungi; EDP52067; EDP52067; AFUB_061010.
DR   VEuPathDB; FungiDB:AFUB_061010; -.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   PhylomeDB; B0Y1V8; -.
DR   Proteomes; UP000001699; 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; Hydrolase; Protease; Secreted; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..70
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q12567"
FT                   /id="PRO_0000407043"
FT   CHAIN           71..395
FT                   /note="Aspergillopepsin-1"
FT                   /id="PRO_0000407044"
FT   DOMAIN          86..392
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        284
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   DISULFID        320..355
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   395 AA;  41613 MW;  F3D1CCC0C6814BA9 CRC64;
     MVVFSKVTAV VVGLSTIVSA VPVVQPRKGF TINQVARPVT NKKTVNLPAV YANALTKYGG
     TVPDSVKAAA SSGSAVTTPE QYDSEYLTPV KVGGTTLNLD FDTGSADLWV FSSELSASQS
     SGHAIYKPSA NAQKLNGYTW KIQYGDGSSA SGDVYKDTVT VGGVTAQSQA VEAASHISSQ
     FVQDKDNDGL LGLAFSSINT VSPRPQTTFF DTVKSQLDSP LFAVTLKYHA PGTYDFGYID
     NSKFQGELTY TDVDSSQGFW MFTADGYGVG NGAPNSNSIS GIADTGTTLL LLDDSVVADY
     YRQVSGAKNS NQYGGYVFPC STKLPSFTTV IGGYNAVVPG EYINYAPVTD GSSTCYGGIQ
     SNSGLGFSIF GDIFLKSQYV VFDSQGPRLG FAPQA