ID   SUB6_TRITO              Reviewed;         412 AA.
AC   Q3ZEJ8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Subtilisin-like protease 6;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB6; Synonyms=ALP1;
OS   Trichophyton tonsurans (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16244893; DOI=10.1007/s11046-005-0132-0;
RA   Bhathena A., Gaedigk R., Abdel-Rahman S.M.;
RT   "Characterization of the ALP1 gene locus of Trichophyton tonsurans.";
RL   Mycopathologia 160:265-272(2005).
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; AY910749; AAX93514.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3ZEJ8; -.
DR   SMR; Q3ZEJ8; -.
DR   VEuPathDB; FungiDB:TESG_02550; -.
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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..127
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380814"
FT   CHAIN           128..412
FT                   /note="Subtilisin-like protease 6"
FT                   /id="PRO_0000380815"
FT   DOMAIN          36..120
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          135..412
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        167
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        198
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        358
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  42971 MW;  F9B9FC36B2621933 CRC64;
     MGFITKAIPI VLAALSTVNG AKILEAGPHA ETIPNKYIVV MKREVSDEAF SAHTTWLSQN
     LNRRVMRRSG SSKAMAGMQD KYSLGGIFRA YSGEFDDAMI KDISSHDDVD YIEPDFVVRT
     STNGTNLTRQ DNVPSWGLAR VSSKKAGGTT YYYDSSAGKG VTAYVIDTGI DINHEDFRGR
     AKWGKNFVDD MDEDCNGHGT HVAGTVGGTK YGLAKGVSLV AVKVLDCEGS GSNSGVIKGM
     EWAMREASGG GNGTAKAAGK AVMNMSLGGT RSQASNQAAK AISDAGIFMA VAAGNENMDA
     QHSSPASEPS VCTVAASTED DGKADFSNYG QLVDVYAPGK DITSLKPGGS TDTLSGTSMA
     SPHVCGLGAY LIGLGKQGGP GLCDTIKEMA HDAIQRPGEG TTSKLIYNGS GK