ID   CARP_ARTBC              Reviewed;         400 AA.
AC   D4B385;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=ARB_02919;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
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; ABSU01000032; EFE30240.1; -; Genomic_DNA.
DR   RefSeq; XP_003010880.1; XM_003010834.1.
DR   AlphaFoldDB; D4B385; -.
DR   SMR; D4B385; -.
DR   STRING; 663331.D4B385; -.
DR   MEROPS; A01.018; -.
DR   PRIDE; D4B385; -.
DR   EnsemblFungi; EFE30240; EFE30240; ARB_02919.
DR   GeneID; 9524995; -.
DR   KEGG; abe:ARB_02919; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   OMA; DKSHYTG; -.
DR   Proteomes; UP000008866; 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   Reference proteome; 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_0000397694"
FT   CHAIN           73..400
FT                   /note="Probable vacuolar protease A"
FT                   /id="PRO_0000397695"
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;  43416 MW;  71570F4A59AE9A2F CRC64;
     MKGSLLLAGA TLLGCTSAKL HSLKLKKVSL KEQLEHADID VQIKSLGQKY MGIRPEQHEQ
     QMFKEQTPIE VESGHNVLID NFLNAQYFSE ISIGTPPQTF KVVLDTGSSN LWVPGKDCSS
     IACFLHSTYD SSASSTYSKN GTKFAIRYGS GSLEGFVSRD SVKIGDMTIK KQLFAEATSE
     PGLAFAFGRF DGIMGMGFSS ISVNGITPPF YNMIDQGLID EPVFSFYLGD TNKDGDQSVV
     TFGGSDTNHF TGDMTTIPLR RKAYWEVDFD AISLGKDTAA LENTGIILDT GTSLIALPTT
     LAEMINTQIG ATKSWNGQYT LDCAKRDSLP DVTFTLSGHN FTIGPHDYTL EVSGTCISSF
     MGMDFPEPVG PLAILGDSFL RRYYSVYDLG KGTVGLAKAK