SUB6_ARTBE
ID SUB6_ARTBE Reviewed; 412 AA.
AC Q64K31;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Subtilisin-like protease 6;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB6;
OS Arthroderma benhamiae (Trichophyton mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=63400;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15363848; DOI=10.1016/j.gene.2004.06.024;
RA Jousson O., Lechenne B., Bontems O., Mignon B., Reichard U., Barblan J.,
RA Quadroni M., Monod M.;
RT "Secreted subtilisin gene family in Trichophyton rubrum.";
RL Gene 339:79-88(2004).
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; AY437857; AAS45671.1; -; Genomic_DNA.
DR AlphaFoldDB; Q64K31; -.
DR SMR; Q64K31; -.
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..127
FT /evidence="ECO:0000255"
FT /id="PRO_0000380806"
FT CHAIN 128..412
FT /note="Subtilisin-like protease 6"
FT /id="PRO_0000380807"
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 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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