ID   SUB9_ARTBC              Reviewed;         402 AA.
AC   D4B5N1;
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 9;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB9; ORFNames=ARB_03790;
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}.
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DR   EMBL; ABSU01000045; EFE29359.1; -; Genomic_DNA.
DR   RefSeq; XP_003015507.1; XM_003015461.1.
DR   AlphaFoldDB; D4B5N1; -.
DR   SMR; D4B5N1; -.
DR   STRING; 63400.XP_003015507.1; -.
DR   EnsemblFungi; EFE29359; EFE29359; ARB_03790.
DR   GeneID; 9525350; -.
DR   KEGG; abe:ARB_03790; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_3_1; -.
DR   OMA; ATSWSNY; -.
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; 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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..120
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000406384"
FT   CHAIN           121..402
FT                   /note="Subtilisin-like protease 9"
FT                   /id="PRO_0000406385"
FT   DOMAIN          36..119
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          130..402
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        162
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        193
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        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   402 AA;  42128 MW;  E90278A77FB7E571 CRC64;
     MGFFRQLFSL SLCALSLAIP SKLIGLENTQ DVIPNSYIVV MKSTISEAEF QTHQAWASKI
     HRRNLGERDG TLGGLDGLKT TFEFEGLKGY SGAFDKRTIE LISRNPAVDY VEVDRVVKLD
     AITTQRNAPS WGLGRISHKS AGSSDFVFDD SAGSGITIYG VDTGIDIKHP EFSGRATWGT
     NTVDNEDTDQ NGHGTHTAGT FAGATYGIAK KANVIAVKVL NAQGTGSTSG VIQGIQWCTD
     HAGRNGLRGK AAMNLSLGIR GSTVFNRVAE AAQQSGIFLA VAAGNDGTDA AQFSPASARG
     VCTAAATNSQ DAATSWSNYG SVVAVYGPGA DIVSAYPNED TATLSGTSMA SPHVCGVGAY
     LMALEGIGPD KVCDRIKELA VESVTNQKPN TTRKLLYNGS GA