ID   CARP_ARTOC              Reviewed;         395 AA.
AC   C5FS55;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=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=MCYG_05527;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
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: 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. Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; DS995705; EEQ32708.1; -; Genomic_DNA.
DR   RefSeq; XP_002845658.1; XM_002845612.1.
DR   AlphaFoldDB; C5FS55; -.
DR   SMR; C5FS55; -.
DR   STRING; 63405.XP_002845658.1; -.
DR   MEROPS; A01.018; -.
DR   EnsemblFungi; EEQ32708; EEQ32708; MCYG_05527.
DR   GeneID; 9224665; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   OMA; DKSHYTG; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000002035; 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; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..72
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000388448"
FT   CHAIN           73..395
FT                   /note="Vacuolar protease A"
FT                   /id="PRO_0000388449"
FT   DOMAIN          87..392
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        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        118..123
FT                   /evidence="ECO:0000250"
FT   DISULFID        318..351
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   395 AA;  43077 MW;  5CF7D93853022B93 CRC64;
     MKGSLLLAGA TLLGCTSAKL HSLKLKKVSL KEQLEHADID VQIKSLGQKY MGIRPGQHEQ
     QMFKEQTPIE AESGHNVLID NFLNAQYFSE ISIGTPPQTF KVVLDTGSSN LWVPGKDCSS
     IACFLHSTYD SSASSTFTRN GTSFAIRYGS GSLEGFVSQD NVQIGDMKIK NQLFAEATSE
     PGLAFAFGRF DGILGMGYDT ISVNKITPPF YKMVEQGLVD EPVFSFYLGD TNKDGDQSVV
     TFGGADKSHY TGDITTIPLR RKAYWEVEFN AITLGKDTAT LDNTGIILDT GTSLIALPTT
     YAEMIISKSW NGQYTIDCAK RDSLPDLTFT LSGHNFTIGP YDYTLEVSGT CISSFMGMDF
     PEPVGPLAIL GDSFLRRWYS VYDLGKGTVG LAKAK