ID   SUB1_TRITO              Reviewed;         507 AA.
AC   B8XGQ4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Subtilisin-like protease 1;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB1;
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].
RA   Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; FJ348236; ACL37326.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8XGQ4; -.
DR   SMR; B8XGQ4; -.
DR   MEROPS; S08.025; -.
DR   VEuPathDB; FungiDB:TESG_01096; -.
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   3: Inferred from homology;
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_0000380761"
FT   CHAIN           117..507
FT                   /note="Subtilisin-like protease 1"
FT                   /id="PRO_0000380762"
FT   DOMAIN          34..113
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          126..400
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REGION          175..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..475
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        190
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        345
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   507 AA;  53080 MW;  7E87C9C527EA2E24 CRC64;
     MGVFRFISIS LAAVSAANAA QILSMPHAQT VPHSYIVMMK DDTSDDDFNH HQSWLQSTHT
     HNITRRATIQ NAGMRHKYNF RKMKGYSGIF DEETIKDIAK DPKVMFVEPD TIISVNGKVE
     QSNVPSWGLA RISNSQPGAN SYVYDSSAGE GITVYSVDTG VDINHEDFEG RAIWGSNQVN
     DGDDRDGSGH GTHTSGTMVG KEFGIAKKAK LVAVKVLGND GSGPTSGIVA GINWCVEHAR
     QNGGTDKAVM NMSLGGSSSS ALNRAAAQAV EQGMFLSVAA GNENQDARSS SPASEPSVCT
     VGSSAEDDSR SSFSNWGPAL DLFAPGSNII SARPGGGSQS MSGTSMAAPH VAGLAAYLMA
     LEGISGGAVC DRLKELGSSS ITDVGPGTPT NVLISNGGAK GGNPKPAPGP SPNPSQPSEP
     QQPAPSQPGE PGESFPGEPF PGEPFPGEPF PGESSPGESA PAPAPMPPSP QHPHTPYPGG
     DNFDFDGYWK KYFGGEHWRK MFGSFWN