ID   PEPA_NEOFI              Reviewed;         395 AA.
AC   A1DDK1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=NFIA_073740;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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}.
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; DS027696; EAW17458.1; -; Genomic_DNA.
DR   RefSeq; XP_001259355.1; XM_001259354.1.
DR   AlphaFoldDB; A1DDK1; -.
DR   SMR; A1DDK1; -.
DR   STRING; 331117.A1DDK1; -.
DR   MEROPS; A01.026; -.
DR   EnsemblFungi; EAW17458; EAW17458; NFIA_073740.
DR   GeneID; 4585962; -.
DR   KEGG; nfi:NFIA_073740; -.
DR   VEuPathDB; FungiDB:NFIA_073740; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   OMA; GFWEFTA; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000006702; 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; Reference proteome;
KW   Secreted; Signal; 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_0000407052"
FT   CHAIN           71..395
FT                   /note="Aspergillopepsin-1"
FT                   /id="PRO_0000407053"
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;  41574 MW;  4893302C2AAF1F8A CRC64;
     MVVFSKVTAV VVGLSTIVSA VPVVQPRKGF TINQVARPVT NKKTVNLPAV YANALTKYGG
     TVPDSVKAAA SSGSAVTTPE QYDSEYLTPV KVGGTTLNLD FDTGSADLWV FSSELSASES
     SGHAIYKPSA NAQKLNGYTW KIQYGDGSGA SGDVYKDTVT VGGVTAQSQA VEAASQISSQ
     FVQDKDNDGL LGLAFSSLNT VSPRPQTTFF DTVKSQLDSP LFAVTLKYHA PGTYDFGYID
     NSKFQGKLTY ADVDNSQGFW MFTADGYGVG DGAPNSNHIS GIADTGTTLL LLDDSVVADY
     YHQVSGAKNS NEYGGYVFPC STKLPSFTTV IGGYNAVVPG EYINYAPVTD GSSTCFGGIQ
     SNSGLGFSIF GDVFLKSQYV VFDSQGPRLG FAPQA