ID   PEPA_ARTGP              Reviewed;         403 AA.
AC   E5R1B9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Aspartic protease pepA {ECO:0000305};
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   ORFNames=MGYG_00710;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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.
CC       {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; DS989822; EFQ97670.1; -; Genomic_DNA.
DR   RefSeq; XP_003176622.1; XM_003176574.1.
DR   AlphaFoldDB; E5R1B9; -.
DR   SMR; E5R1B9; -.
DR   STRING; 63402.XP_003176622.1; -.
DR   EnsemblFungi; EFQ97670; EFQ97670; MGYG_00710.
DR   GeneID; 10031942; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   InParanoid; E5R1B9; -.
DR   OMA; YGSGNAK; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000002669; 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   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..67
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q12567"
FT                   /id="PRO_0000407037"
FT   CHAIN           68..403
FT                   /note="Aspartic protease pepA"
FT                   /id="PRO_0000407038"
FT   DOMAIN          82..400
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        329..362
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   403 AA;  42821 MW;  8F414BB3FDC06A84 CRC64;
     MVLITQLGAA LAVFSALTVA APTKGKARFS APQVGIPKKA KHHPAAAYAR ALHKFGMKIP
     KAVSDAAKGS VPTTPTQNDE QYVTQVTVGG STLNLDLDTG SADLWVFSTE TPQDESQGHN
     IYKPSSGAKR LDGYSWEIKY GDSSSAHGDV FLDTVTVGGV TTSSQAVESA KEVSSQFVKD
     KATDGLMGLS FSVLNTVQPQ PQKTFFDNVL SQLEQPLFTC TLKHGEPGTY DFGYIDDSKH
     TGEIAYTQVD NSNGWWGFTA DGYSIGGGSN SSYSLYGAQH KRANGGSISG IADTGTTLML
     LSDDVVGDYY QNVQGATQDQ MQGGWVFPCD ANLPDFILNI GGYNAVVPGK FMNFQEIDNS
     MCFGGLQSSG GGSTPNIFGD VFLKSQFVVW DTQGPRIGFA PQA