ID   SUB3_ARTOT              Reviewed;         397 AA.
AC   Q8J0D7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Subtilisin-like protease 3;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB3;
OS   Arthroderma otae (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=63405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IHEM 15221;
RX   PubMed=12406327; DOI=10.1046/j.1523-1747.2002.01784.x;
RA   Descamps F., Brouta F., Monod M., Zaugg C., Baar D., Losson B., Mignon B.;
RT   "Isolation of a Microsporum canis gene family encoding three subtilisin-
RT   like proteases expressed in vivo.";
RL   J. Invest. Dermatol. 119:830-835(2002).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=15363848; DOI=10.1016/j.gene.2004.06.024;
RA   Jousson O., Lechenne B., Bontems O., Mignon B., Reichard U., Barblan J.,
RA   Quadroni M., Monod M.;
RT   "Secreted subtilisin gene family in Trichophyton rubrum.";
RL   Gene 339:79-88(2004).
CC   -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC       activity that contributes to pathogenicity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15363848}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AJ431180; CAD24010.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J0D7; -.
DR   SMR; Q8J0D7; -.
DR   MEROPS; S08.115; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..116
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000068280"
FT   CHAIN           117..397
FT                   /note="Subtilisin-like protease 3"
FT                   /id="PRO_5000068281"
FT   DOMAIN          35..116
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          126..397
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        189
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        344
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   397 AA;  40855 MW;  BB09E91E4D987B31 CRC64;
     MGCIKVISVF LAAVAAVDAR AFFHNRGGND VIPNSYIVVM KDGVTAEDFD SHISSVATTH
     SINKAKRGSE TVGHKDSFNI NGWRAYNGHF DEATIESILN DDKVDYVEHD RVVKLAALTT
     QPNAPTWGLG RVSHKAPGNK DFVYDSSAGQ GVTIYGVDTG IDINHPEFRG RIRWGTNTVD
     NDNTDGNGHG THTAGTFAGT TYGVAKKANI VAVKVLSAGG SGSTAGVIKG IDWCVTDAKA
     KGALGKAALN LSLGGAFSQA NNDAVTRAQN AGIFVAVAAG NDNKDAKNSS PASAPAVCTA
     ASSTIDDQKS SFSNWGTIVD IYAPGSNILS AAPGGGTRTL SGTSMASPHV CGVGAAMLAQ
     GVSVAQACDR IKQIANAVIK NPGTGTTNKL LYNGSGR