ID   SUB2_TRIRU              Reviewed;         421 AA.
AC   Q69F57;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Subtilisin-like protease 2;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB2;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR11461.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY343500; AAR11461.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q69F57; -.
DR   SMR; Q69F57; -.
DR   MEROPS; S08.115; -.
DR   VEuPathDB; FungiDB:TERG_08260; -.
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; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
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; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..122
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380770"
FT   CHAIN           123..421
FT                   /note="Subtilisin-like protease 2"
FT                   /id="PRO_0000380771"
FT   DOMAIN          36..121
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          131..421
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        357
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   421 AA;  45764 MW;  CB52151989E48C6A CRC64;
     MQLLNFGLLL LPFVAGDLAP QPEPLLVGPS DIVPGQYLVT LKEGLTSAQI RDHKKWVSSV
     HRANLDSFAA GARGVETEGI MKHFHIHDLN MYSGGFDEKR VEDLSRSPYV KSVHPDQHFY
     LAKTVTQRQA RWGLGYMSSK GKPVPLHSTL VDYSYDDKAG EGVWAYVLDT GINVNHVEFE
     GRAILGHNAI PNKSHTDEFG HGTCVAGIIA GKTYGVAKKA NVVSAKAFDT GSSTYNYILE
     TYDWIIRNIT DSNRKNKAVI NLSISGAKYQ PFDDAAERAF KAGITTVVAA GNDGKDAKNN
     TPASSPNAIT VGAVRWENTR PSFSNYGKIV DIWAPGELIK SCWKGGNNAT STQSGTSAAS
     PHVAGLVAYL MSIKNLPSPS AVTARVLNLT IPNLVKDAKD SPNRVVYNGI QERKCKLPKY
     Y