ID   SUB5_TRIRU              Reviewed;         396 AA.
AC   Q69F34;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Subtilisin-like protease 5;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB5;
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 moderately increased during growth on protein-
CC       rich medium. Expression levels are the same whether keratin is present
CC       or not in the protein-rich medium. {ECO:0000269|PubMed:19098130}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AY344482; AAR02424.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q69F34; -.
DR   SMR; Q69F34; -.
DR   PRIDE; Q69F34; -.
DR   VEuPathDB; FungiDB:TERG_08201; -.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..116
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380800"
FT   CHAIN           117..396
FT                   /note="Subtilisin-like protease 5"
FT                   /id="PRO_0000380801"
FT   DOMAIN          37..113
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          125..396
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REGION          376..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        156
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        187
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        342
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   396 AA;  41793 MW;  3915F6009CEDBD57 CRC64;
     MTGFFTILSF SLAALSVTNA AQILSVPKGA EVVPNGYIVV MKDDTSQQDF SSHRVWISSI
     HHNMTRRGLD GAGVKQTYDF DHLRGYSGIF DEDTIKDISN DPKVAFVEPD AIISQHVVVQ
     QRKAPWGLSR LSNRRGGRNY VFDSSAGSGV WAYVVDSGVD IRHSEFQGRA VWGSNLVDNK
     NSDGTGHGTH VAGTIAGKTY GIAKKAKVVA VKVLNSEGKG PTSGIIAGIN WSIRHARKHG
     MLQKSVLNMS LGGTYSAGLN HATAQAIKAG MFVSVSAGND NINSNGNSPA SERSVCTIAA
     STENDGKASF SNWGPAVDLY APGHNILSAR PGGGSQTMSG TSMAAPHAAG VAAYLIAKEG
     IPGNRACLRL KQLSQPTIRN PGPDTTSRLL YNGSGR