ID   SUB1_TRIRU              Reviewed;         504 AA.
AC   Q69F58;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Subtilisin-like protease 1;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB1;
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).
RN   [2]
RP   INDUCTION.
RX   PubMed=19098130; DOI=10.1128/ec.00208-08;
RA   Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J.,
RA   Bueno M., Giddey K., Staib P.;
RT   "Gene expression profiling in the human pathogenic dermatophyte
RT   Trichophyton rubrum during growth on proteins.";
RL   Eukaryot. Cell 8:241-250(2009).
CC   -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC       activity that contributes to pathogenicity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Expression is strongly increased during growth on protein-
CC       rich medium containing keratin. {ECO:0000269|PubMed:19098130}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AY343499; AAR11460.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q69F58; -.
DR   SMR; Q69F58; -.
DR   MEROPS; S08.025; -.
DR   PRIDE; Q69F58; -.
DR   VEuPathDB; FungiDB:TERG_03400; -.
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   2: Evidence at transcript level;
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_0000380759"
FT   CHAIN           117..504
FT                   /note="Subtilisin-like protease 1"
FT                   /id="PRO_0000380760"
FT   DOMAIN          34..116
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          172..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..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..472
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        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   504 AA;  52815 MW;  207D8F20C762CEA7 CRC64;
     MGVFRFISIS LAAVSAANAA QILSMPHAQT VPNSYIVMMK DDTSDDDFKH HQSWLQSTHT
     HNITRRATIQ NAGMRHKYNF NKMKGYSGIF DDETIKDIAK DPKVMFVEPD TIVSVHGKVE
     QSNVPSWGLA RISNPQPGAD SYTYDSSAGE GITVYSVDTG VDVNHEDFEG RAIWGSNQVN
     DGDDRDGSGH GTHTSGTMVG KMYGIAKKAK LVAVKVLGND GSGPTSGIVA GINWSVEHAR
     QNGGTKKAVM NMSLGGSSSS ALNRAAAQAV EQGMFLSVAA GNDNQDAQSS SPASEPSVCT
     VGSSAEDDSR SSFSNWGPAI DIFAPGSNIV SARPGGGSQS MSGTSMAAPH VAGLAAYLMA
     LEGISGGAVC DRLKELGTSS ITDAGPGTPT NVLINNGGAK GGQPNPNPAP APSPSQPSEP
     QQPTPSQPGQ PGEPFPGEPF PGEPFPGQPF PGESAPAPAP APMPPTPQHP HTPYPGGDNF
     DFDSFWKKYF GGEHWRKMFS SFWN