ID   OPSB_TRIVH              Reviewed;         495 AA.
AC   D4DFT3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Probable aspartic-type endopeptidase OPSB;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=OPSB; ORFNames=TRV_06035;
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: Probable GPI-anchored aspartic-type endopeptidase which
CC       contributes to virulence. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; ACYE01000341; EFE39309.1; -; Genomic_DNA.
DR   RefSeq; XP_003019933.1; XM_003019887.1.
DR   AlphaFoldDB; D4DFT3; -.
DR   SMR; D4DFT3; -.
DR   EnsemblFungi; EFE39309; EFE39309; TRV_06035.
DR   GeneID; 9584685; -.
DR   KEGG; tve:TRV_06035; -.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR47965; PTHR47965; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..467
FT                   /note="Probable aspartic-type endopeptidase OPSB"
FT                   /id="PRO_0000397710"
FT   PROPEP          468..495
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000397711"
FT   DOMAIN          73..408
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          448..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   LIPID           467
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   495 AA;  51834 MW;  0CDC5C38AD3AC9D5 CRC64;
     MRGDSFIWSL ATAIPLLSTA VESLKVVKRD NPSVLGFDIE RFQAAKPVHR DIIAKRASTK
     TISQDLDNQK NLYFCNLTLG TPPQTIRAHI DTGSSDLWVN TAESRFCSSR RAPCSQGGTY
     DSSSSSTYQL VNNDFNISYV DGSGATGDYV TDVINVGGIK LKDFQFAIGH TSSSPLGVLG
     IGYEAGEAQV TRSGDQSYPN LPAALVKAGH IRSNAYSLWL NDLSASRGQI LFGGIDTGKF
     QGKLQTVPVL HTSRGDYTSL VVALTGVGIR TGSDGSIDTF PSQPVAVAMD SGSSLSYLPD
     ALAAKVYNSV DAVFDPANNL AFVPCSMAND KRKLVFTFSS PQIAVGMDEL VIDLGPDANG
     NEATFRDGSK ACVFGIAPAG SSISILGDTV LRSAYLVYDL DNNEISIAPT RFNSTETNIM
     EIGTGENSVP DATGVPNAVT SAQVTQATGL PGVETGVPGS RPPSSKAAGQ AKRPDFVLGV
     AAVGLAGAGM LFAAM