ID   SUB7_TRIVO              Reviewed;         400 AA.
AC   A1XIH6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Subtilisin-like protease 7;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB7;
OS   Trichophyton violaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=LAU 209;
RX   PubMed=17156126; DOI=10.1111/j.1574-6968.2006.00541.x;
RA   Giddey K., Favre B., Quadroni M., Monod M.;
RT   "Closely related dermatophyte species produce different patterns of
RT   secreted proteins.";
RL   FEMS Microbiol. Lett. 267:95-101(2007).
CC   -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC       activity that contributes to pathogenicity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17156126}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; DQ382275; ABD38561.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1XIH6; -.
DR   SMR; A1XIH6; -.
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; 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; PS00137; SUBTILASE_HIS; 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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..119
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380828"
FT   CHAIN           120..400
FT                   /note="Subtilisin-like protease 7"
FT                   /id="PRO_0000380829"
FT   DOMAIN          36..118
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          129..400
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        161
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        192
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        346
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   400 AA;  41549 MW;  C0F126E24E103AF7 CRC64;
     MGFITKAIPL ALAAASVING AEILETRAGV QTLADKYIVV MNDGISDKDF DSHRSWVNRN
     HRRRLIRRGA KAMGGMKHTY NFPTGLKGYS GHFDEQMINE ISKRADVKYI ERDARVQINA
     IEQQDNVPSW GLARVGSKEP GGTTYYYDST AGEGSTAYVI DTGTDIQHEE FEGRATWGAN
     FVDDMDMDCN GHGTHVSGTI GGKTFGVAKK SNVVAVKVLD CSGSGSNSGV IMGMEWATKD
     AQQKGADKAV ANMSLGGAFS QASNDAAAAI AKGGVFLAVA AGNDNVDAAD SSPASEPSIC
     TIAASTEQDS KADFSNFGQV VDVYAPGDSI TSAKPGGGSQ VLSGTSMATP HVAGLGAYLI
     GLGKGGGPGL CDTIKQMAID VIQNPGASTT SKLINNGSGM