ID   SUB10_ARTBC             Reviewed;         522 AA.
AC   D4AQG0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Subtilisin-like protease 10;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB10; ORFNames=ARB_06467;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE34704.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000005; EFE34704.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_003015344.1; XM_003015298.1.
DR   AlphaFoldDB; D4AQG0; -.
DR   SMR; D4AQG0; -.
DR   STRING; 63400.XP_003015344.1; -.
DR   EnsemblFungi; EFE34704; EFE34704; ARB_06467.
DR   GeneID; 9521068; -.
DR   KEGG; abe:ARB_06467; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_3_1; -.
DR   Proteomes; UP000008866; 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; Reference proteome; Secreted;
KW   Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..117
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000406392"
FT   CHAIN           118..522
FT                   /note="Subtilisin-like protease 10"
FT                   /id="PRO_0000406393"
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          384..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..410
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;  55200 MW;  2A1084B7246AF88C CRC64;
     MFFFKGVVAV LSFFSAVNAA PFMKPNNGTR NYIPDSYIVL LKRDISHDDF ELHKRWASDV
     HKRDVAKRGI SFSGIGHSWA TGSFRGYSGV FSRDTIEEIM KHEHVAHVER DQIGTSQGWV
     TQSGAPNWGL GRLSNNSPGN TDYTYDENAG GNGVVYVIDS GIDTMHPEFQ GRATWGANFI
     DKNNVDCWNH GTHCAGIIGS ATFGVAKLTA LIAVKVLDCN GQGPYSAFVA GLHWATKHAQ
     DNGFIGRAII NFSLGGDNSP AVNQALEEAQ RAGIFVSAAA GNFGSDAGSI TPGGAGLICV
     IGNSDDRDYR WTGQGPSNFG ARVDIFAPGT NILSTIPGGG SGVMTGTSMA APHVAGQAAI
     LASISGSGFD LGAACAFFKN SASASVKNPG PNTTNKLLVN GANGTKGPKQ GENKPNKPPG
     QDEQPGQNKP PSQNPPPGQN PPPGQNPPPE QPAPSPPANP GDEPNPDGQP YPGDQPNPGD
     SGPSWWMPSG GLQPPAWWNR RPSFGGWNRP MWWNRPLSVW KL