ID   SUB6_ARTBC              Reviewed;         412 AA.
AC   D4ALV9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Subtilisin-like protease 6;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB6; ORFNames=ARB_05307;
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).
RN   [2]
RP   INDUCTION.
RX   PubMed=19942661; DOI=10.1099/mic.0.033464-0;
RA   Staib P., Zaugg C., Mignon B., Weber J., Grumbt M., Pradervand S.,
RA   Harshman K., Monod M.;
RT   "Differential gene expression in the pathogenic dermatophyte Arthroderma
RT   benhamiae in vitro versus during infection.";
RL   Microbiology 156:884-895(2010).
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 highly up-regulated during infection.
CC       {ECO:0000269|PubMed:19942661}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; ABSU01000002; EFE36368.1; -; Genomic_DNA.
DR   RefSeq; XP_003017013.1; XM_003016967.1.
DR   AlphaFoldDB; D4ALV9; -.
DR   SMR; D4ALV9; -.
DR   STRING; 63400.XP_003017013.1; -.
DR   EnsemblFungi; EFE36368; EFE36368; ARB_05307.
DR   GeneID; 9526734; -.
DR   KEGG; abe:ARB_05307; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_3_1; -.
DR   OMA; CEGSGSN; -.
DR   PHI-base; PHI:6569; -.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..127
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397798"
FT   CHAIN           128..412
FT                   /note="Subtilisin-like protease 6"
FT                   /id="PRO_0000397799"
FT   DOMAIN          36..120
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          135..412
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        167
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        198
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        358
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  42735 MW;  258C909A68A7AF37 CRC64;
     MGFITKAIPI VLAALSTVNG ARILEAGPHA ETIPNKYIVV MKKDVSEEAF SAHTTWLSQT
     LNSRLMRRAG SSKPMAGMQD KYSLGNVFRA YSGEFDEAMI KDISGHDDVD FIEPDFVVRT
     TTNGTNLTHQ DNVPSWGLAR VGSKQAGGTT YYYDPSAGKG VRAYIIDTGI DTDHKDFGGR
     AKWGKNFADD MDQDCNGHGT HVAGTVGGTQ YGLAKSVSLI AVKVLDCEGS GSNSGVIKGM
     EWAMRDASGG GNGTAKAAGK TVMNMSLGGP RSEATNQAAK AISDAGIFLA VAAGNENMDA
     QHSSPASEPS VCTVAASTKD DGKASFSNYG SAVDVYAPGK DITSLKPGGS TDTLSGTSMA
     SPHVCGLGAY LIGLGKQGGP GLCDTIKEMA NDAIQSPGED TTSKLIYNGS GK