SUB6_TRISH
ID SUB6_TRISH Reviewed; 405 AA.
AC Q8J077;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Subtilisin-like protease 6;
DE EC=3.4.21.-;
DE AltName: Allergen=Tri m 2;
DE Flags: Precursor; Fragment;
GN Name=SUB6; Synonyms=tri m 2;
OS Trichophyton schoenleinii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=34386;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CBS 433.63, VKPGF 232/181, and VKPGF 235/25;
RA Probst S., Polyakov I., Ivanova L., Graeser Y.;
RT "Development of DNA markers to explore the genetic relatedness of strains
RT of the two dermatophyte species causing Favus of human and mouse.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC activity that contributes to pathogenicity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AJ430841; CAD23616.1; -; Genomic_DNA.
DR EMBL; AJ430842; CAD23617.1; -; Genomic_DNA.
DR EMBL; AJ430843; CAD23618.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8J077; -.
DR SMR; Q8J077; -.
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 1: Evidence at protein level;
KW Allergen; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Virulence; Zymogen.
FT SIGNAL <1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..125
FT /evidence="ECO:0000250"
FT /id="PRO_0000397800"
FT CHAIN 126..>405
FT /note="Subtilisin-like protease 6"
FT /id="PRO_0000397801"
FT DOMAIN 34..118
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 133..405
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 356
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 405
SQ SEQUENCE 405 AA; 42263 MW; AA0ABC90FF68004F CRC64;
FITKAIPIVL AALSAVNGAK ILEAGPHAET IPNKYIVVMK KDVSDEAFST HTTWLSQNLN
RRLMRRSGSS KAMAGMQNKY SLGGIFRAYS GEFDDAMIKD ISNHDDVDYI EPDFVVRTST
NGTNLTRQEN VPSWGLARVG SKQAGGTTYY YDSSAGKGVT AYVIDTGIDI EHEDFGGRAK
WGKNFVDQRD EDCNGHGTHV AGTVGGTKYG LAKSVSLVAV KVLDCDGSGS NSGVIRGMEW
AMREASGGGN GTAKAAGKSV MNMSLGGPRS QASNDAARAI SEAGIFMAVA AGNENMDAQH
SSPASEPSVC TVAASTEDDG KAEFSNYGAV VDVYAPGKDI TSLKPGGSTD TLSGTSMASP
HVCGLGAYLI GLGKQGGPGL CDTIKQMANE AIQRPGEGTT GKLIY