ID   SUB2_TRIVH              Reviewed;         421 AA.
AC   D4DLI5; D4DEN0;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Subtilisin-like protease 2;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB2; ORFNames=TRV_08059/TRV_05599;
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: 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}.
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DR   EMBL; ACYE01000509; EFE37294.1; -; Genomic_DNA.
DR   EMBL; ACYE01000301; EFE39705.1; -; Genomic_DNA.
DR   RefSeq; XP_003017939.1; XM_003017893.1.
DR   RefSeq; XP_003020323.1; XM_003020277.1.
DR   AlphaFoldDB; D4DLI5; -.
DR   SMR; D4DLI5; -.
DR   EnsemblFungi; EFE37294; EFE37294; TRV_08059.
DR   EnsemblFungi; EFE39705; EFE39705; TRV_05599.
DR   GeneID; 9579815; -.
DR   GeneID; 9584062; -.
DR   KEGG; tve:TRV_05599; -.
DR   KEGG; tve:TRV_08059; -.
DR   HOGENOM; CLU_011263_6_3_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
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_0000397784"
FT   CHAIN           123..421
FT                   /note="Subtilisin-like protease 2"
FT                   /id="PRO_0000397785"
FT   DOMAIN          36..122
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        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;  45636 MW;  AEA0DFAA15271232 CRC64;
     MQLLNFGLLL LPFVAGDLAP QPEPLLAGPS DVVPGQYIVT LKEGLTSAQI RDHKKWVSSV
     HRANLDSFAA GASGVETEGI MKHFHIHDLN MYSGGFDEKT VEDLSRNPYV KSVHPDQHVY
     LAKTVTQRQA RWGLGYMSSK GKPVPLHSTL VDYSYDDKAG EGVWAYVLDT GINVNHIEFE
     GRAILGHNAI PNKPHTDEFG HGTYVAGIIA GKTYGVAKKA NVVSAKAFDT GSSTYNYILE
     TYDWIVRNIT DSNRKNKAVI NLSISGAKYQ PFDDAVEKAF KAGITTVVAA GNDGKDAKNN
     TPASSPNAIT VGAVRWENTR PSFSNYGKLV DIWAPGELIK SCWKGGNNAT STQSGTSAAS
     PHVAGLVAYL MSIENLPSPS AVTARVLNLT IPNLVKDAKD SPNRVAYNGI QERKFTLPKY
     Y