ID   SUB5_TRIVH              Reviewed;         396 AA.
AC   D4D0F5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Subtilisin-like protease 5;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB5; ORFNames=TRV_00550;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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; ACYE01000031; EFE44662.1; -; Genomic_DNA.
DR   RefSeq; XP_003025273.1; XM_003025227.1.
DR   AlphaFoldDB; D4D0F5; -.
DR   SMR; D4D0F5; -.
DR   EnsemblFungi; EFE44662; EFE44662; TRV_00550.
DR   GeneID; 9582890; -.
DR   KEGG; tve:TRV_00550; -.
DR   HOGENOM; CLU_011263_1_3_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
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..116
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397796"
FT   CHAIN           117..396
FT                   /note="Subtilisin-like protease 5"
FT                   /id="PRO_0000397797"
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        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;  41763 MW;  5102577CB2815B97 CRC64;
     MTGFFTILSF SLAALSVTNA AQILSVPKGA EVVPNGYIVV MKDDTSQQDF SSHRVWISSI
     HHNMTRRGLD GAGVKQTYDF DHLRGYSGIF DEDTIKDISN DPKVAFVEPD AIISQHVVVQ
     QRKAPWGLSR LSNRRGGRNY VFDSSAGSGV WAYVVDSGVD VRHAEFQGRA VWGSNLVDNK
     NSDGTGHGTH VAGTIAGKTY GIAKKAKVVA VKVLNSEGKG PTSGIIAGIN WSIRHARKHG
     MLQKSVLNMS LGGTYSAGLN HATAQAIKAG MFVSVSAGND NINSNGNSPA SERSVCTIAA
     STENDGKASF SNWGPAVDLY APGHNILSAR PGGGSQTMSG TSMAAPHAAG VAAYLIAKEG
     IPGNRACLRL KQLSQPTIRN PGPDTTSRLL YNGSGR