ID   SUB10_TRIVH             Reviewed;         522 AA.
AC   D4DIS6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Subtilisin-like protease 10;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB10; ORFNames=TRV_07087;
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; ACYE01000412; EFE38250.1; -; Genomic_DNA.
DR   RefSeq; XP_003018895.1; XM_003018849.1.
DR   AlphaFoldDB; D4DIS6; -.
DR   SMR; D4DIS6; -.
DR   EnsemblFungi; EFE38250; EFE38250; TRV_07087.
DR   GeneID; 9580066; -.
DR   KEGG; tve:TRV_07087; -.
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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..117
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000406396"
FT   CHAIN           118..522
FT                   /note="Subtilisin-like protease 10"
FT                   /id="PRO_0000406397"
FT   DOMAIN          36..113
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          127..405
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REGION          383..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..477
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        159
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        348
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"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   522 AA;  55393 MW;  9EE80335D078BA1A CRC64;
     MFFFKGVVAV LSFFSAVNAA PFMKPNNGTG KYIPDSYIVL LKRDISHDDF ELHKRWASDV
     HKRDVAKRGI SFSGIGHSWA TGSFRGYSGV FSRDTIEEIM KHEHVAHVER DQIGTSQGWV
     TQPKAPNWGL GRLSNSNPGN TDYTYDEGAG GNAVVYVIDS GIDTMHPEFQ GRATWGANFI
     DKNNVDCWGH GTHCAGIIGS VTFGVAKRAA MIAVKVLDCN GQGPYSAFIA GLHWATEHAQ
     KNGHIGRAII NFSLGGDNSP AVNQALEEAQ KAGIFVSAAA GNFGSDAGSI TPGGARLVCV
     IGNSDERDYR WTGQGPSNFG ARVDIFAPGT DIMSTLPGGG SGVMTGTSMA APHVAGQAAI
     QVSISGGGFD LSVACAFFKN SASASVKNPG PNTTNKLLVN GANGTKGPKQ DENKPNKPPG
     QDEQPGQNKP PSQNPPPGQN PPPGQNPPPE QPAPSPPANP GDEPNPDGQP YPGDQPNPGD
     SGPSWWMPSG GLQPPAWWNR RPSFGGWNRP MWWNRPLSVW KL