ID   PEPA_TRIVH              Reviewed;         403 AA.
AC   D4D7C5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Aspartic endopeptidase PEP1;
DE            EC=3.4.23.18;
DE   AltName: Full=Aspergillopepsin I;
DE   Flags: Precursor;
GN   Name=PEP1; ORFNames=TRV_03007;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation of
CC       proteinaceous substrates. Can catalyze hydrolysis of the major
CC       structural proteins of basement membrane, elastin, collagen, and
CC       laminin. Thought to play a significant role in virulence (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Can catalyze hydrolysis of the major structural proteins of
CC       basement membrane, elastin, collagen, and laminin. Thought to play a
CC       significant role in virulence (By similarity). {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; ACYE01000156; EFE42250.1; -; Genomic_DNA.
DR   RefSeq; XP_003022868.1; XM_003022822.1.
DR   AlphaFoldDB; D4D7C5; -.
DR   SMR; D4D7C5; -.
DR   PRIDE; D4D7C5; -.
DR   EnsemblFungi; EFE42250; EFE42250; TRV_03007.
DR   GeneID; 9581589; -.
DR   KEGG; tve:TRV_03007; -.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   Proteomes; UP000008383; 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; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Secreted; Signal; Virulence; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..67
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397714"
FT   CHAIN           68..403
FT                   /note="Aspartic endopeptidase PEP1"
FT                   /id="PRO_0000397715"
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:PRU10094"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        329..361
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   403 AA;  43002 MW;  CFACE6455EB7D95A CRC64;
     MVQISQIGAV LAVCSTLTVA APTKGKARFN VPQVAVPMKA VHHPAVAYAR ALHKFGMKVP
     KAVSDAARGS VPTTPTKDDE QYVTQVTVGQ GKLNLDLDTG SGDLWVFSTE TPKDQSQGHN
     LYMPTSKSKR LDGYSWEITY GDMSSAGGDV FLDTVSIGNV TASSQAVESA KKVSDQFAKD
     KATDGLMGLS FSVLNTVQPK PQTTFFDTVL KQLEKPLFTC TLKHGQPGSY DFGYIDDSKH
     SGEIAYTNVD NSQGWWGFTA ESYSIGGGSN STHSFHGAQH HGARGSSIDG IADTGTTLML
     LSDDVVQEYY KQVQGAKNDQ QQGGWVFPCD AKLPDFTLSI SGYNAVVPGK FMNYQAVGSV
     CFGGLQSVGS SGGVPNIFGD VFLKSQFVVW DTEGPRIGFA PQA