ID   CARP_TRIVH              Reviewed;         400 AA.
AC   D4DEN7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Probable vacuolar protease A;
DE            EC=3.4.23.25;
DE   AltName: Full=Aspartic endopeptidase PEP2;
DE   AltName: Full=Aspartic protease PEP2;
DE   Flags: Precursor;
GN   Name=PEP2; ORFNames=TRV_05606;
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: Vacuolar aspartic endopeptidase which is probably also
CC       secreted and contributes to virulence. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity for peptide
CC         bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate.
CC         Does not act on esters of Tyr or Arg.; EC=3.4.23.25;
CC   -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000250}. Secreted
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; ACYE01000304; EFE39677.1; -; Genomic_DNA.
DR   RefSeq; XP_003020295.1; XM_003020249.1.
DR   AlphaFoldDB; D4DEN7; -.
DR   SMR; D4DEN7; -.
DR   MEROPS; A01.018; -.
DR   EnsemblFungi; EFE39677; EFE39677; TRV_05606.
DR   GeneID; 9584044; -.
DR   KEGG; tve:TRV_05606; -.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005775; C:vacuolar lumen; 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   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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; Vacuole; Virulence; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..72
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397696"
FT   CHAIN           73..400
FT                   /note="Probable vacuolar protease A"
FT                   /id="PRO_0000397697"
FT   DOMAIN          87..397
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        118..123
FT                   /evidence="ECO:0000250"
FT   DISULFID        323..356
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  43361 MW;  C2A8835A76655749 CRC64;
     MKGSLLLAGA TLLGCTSAKL HSLKLKKVSL KEQLEHADID VQIKSLGQKY MGIRPEQHEQ
     QMFKEQTPIE AESGHNVLID NFLNAQYFSE ISIGTPPQTF KVVLDTGSSN LWVPGKDCSS
     IACFLHSTYD SSASSTYSKN GTKFAIRYGS GSLEGFVSQD SVKIGDMTIK NQLFAEATSE
     PGLAFAFGRF DGIMGMGFSS ISVNGITPPF YNMIDQGLID EPVFSFYLGD TNKEGDQSVV
     TFGGSDTKHF TGDMTTIPLR RKAYWEVDFD AISLGEDTAA LENTGIILDT GTSLIALPTT
     LAEMINTQIG ATKSWNGQYT LDCAKRDSLP DVTFTVSGHN FTIGPHDYTL EVSGTCISSF
     MGMDFPEPVG PLAILGDSFL RRYYSVYDLG KGTVGLAKAK