ID   OPSB_ARTBC              Reviewed;         495 AA.
AC   D4AIS3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Probable aspartic-type endopeptidase OPSB;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=OPSB; ORFNames=ARB_04170;
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: 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; ABSU01000001; EFE36646.1; -; Genomic_DNA.
DR   RefSeq; XP_003017291.1; XM_003017245.1.
DR   AlphaFoldDB; D4AIS3; -.
DR   SMR; D4AIS3; -.
DR   STRING; 663331.D4AIS3; -.
DR   EnsemblFungi; EFE36646; EFE36646; ARB_04170.
DR   GeneID; 9524399; -.
DR   KEGG; abe:ARB_04170; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   OMA; LYFMGGV; -.
DR   Proteomes; UP000008866; 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; Reference proteome; Signal; Virulence;
KW   Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..467
FT                   /note="Probable aspartic-type endopeptidase OPSB"
FT                   /id="PRO_0000397702"
FT   PROPEP          468..495
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000397703"
FT   DOMAIN          73..408
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          447..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;  51858 MW;  C7FAFBC7AB45BCCD CRC64;
     MRGDSFIWSL ATAIPLLSTA VESLQVVKRD NPSVLGFDIE RFQVAKPIHR 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 RFNSTETNIL
     EIGTGENSVP DATGVPNAVT SAQVTQATGL PGVETGVPGS RPPSSKAAGQ AKRPDFVLGV
     AAVGLAGAGM LFAAM