ID   OPSB_ARTOC              Reviewed;         479 AA.
AC   C5FRQ0;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Probable aspartic-type endopeptidase OPSB;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=OPSB; ORFNames=MCYG_05372;
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: 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; DS995705; EEQ32553.1; -; Genomic_DNA.
DR   RefSeq; XP_002845503.1; XM_002845457.1.
DR   AlphaFoldDB; C5FRQ0; -.
DR   SMR; C5FRQ0; -.
DR   STRING; 63405.XP_002845503.1; -.
DR   EnsemblFungi; EEQ32553; EEQ32553; MCYG_05372.
DR   GeneID; 9228711; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   OMA; SEGTFCF; -.
DR   OrthoDB; 753343at2759; -.
DR   Proteomes; UP000002035; 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..451
FT                   /note="Probable aspartic-type endopeptidase OPSB"
FT                   /id="PRO_0000397708"
FT   PROPEP          452..479
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000397709"
FT   DOMAIN          58..393
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          435..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000250"
FT   LIPID           451
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   479 AA;  50266 MW;  011657B4CA52CD7C CRC64;
     MRGDSFIWSL TTAASLLYAT VESLQVVKRD NPSIVGFDIE RFQVAKPVHR DIIAKRASGK
     TVSQDLDNQT IRAHIDTGSS DLWVNTDDSQ FCSSRRSPCR EGGTFDSSSS STYQLVSNDF
     NISYVDGSGA SGDYVTDVIE VGGIQLKEFQ FAIGHTSSSP LGVLGIGYEA GEALVSRFGD
     ESYPNLPAAL VKAGHIRSNA YSLWLNDLSA SRGQILFGGV DTGKFEGKLQ TVPVLHTSGG
     DYTSLVIALT SVGIRTASEG SLDTFPAQPV AVAMDSGSSL SYLPDALAAK IYNSIDAVFD
     PSNNLAFVPC SMVNDDRKLV FTFSSPQITV GMDELVIDLG PDANGNEATF RDGSKACVFG
     IAPAGRSISI LGDTVLRSAY LVYDLDNNEI SIAPTRFNST VTNIMEIGTG KNSVPDATGV
     PNAVTSAPIT QATGLSGIET GVPGARPTSR GAAPTMRPDV TFGVAAAGLA GAGILFAFM