SUB7_TRIVC
ID SUB7_TRIVC Reviewed; 400 AA.
AC Q5VJ71;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Subtilisin-like protease 7;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB7;
OS Trichophyton verrucosum (Cattle ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=63417;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jousson O., Monod M.;
RT "Subtilisin-like proteases gene family in Dermatophytes.";
RL Submitted (OCT-2003) 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 -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AY439111; AAS45679.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5VJ71; -.
DR SMR; Q5VJ71; -.
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; 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; 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..119
FT /evidence="ECO:0000250"
FT /id="PRO_0000380830"
FT CHAIN 120..400
FT /note="Subtilisin-like protease 7"
FT /id="PRO_0000380831"
FT DOMAIN 36..118
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 129..400
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
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 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 400 AA; 41581 MW; 94B96B5D3DEFA73E CRC64;
MGFITKAIPL ALAAASVING AEIMETRAGV QTLADKYIVV MNDGMTDKDF DSHRSWVNRT
HRRRLIRRGA KAMGGMKHTY RFPTGLKGYS GHFDEQMINE ISKRADVKYI ERDARVQINA
IEQQDNVPSW GLARVGSKEP GGTTYYYDGT AGEGSTAYVI DTGTDIQHEE FEGRATWGAN
FVDDMDMDCN GHGTHVSGTI GGKTFGVAKK SNVVAVKVLD CNGSGSNSGV IMGMEWATKD
AQQKGADKAV ANMSLGGAFS QASNDAAAAI AQGGVFLAVA AGNDNVDAAD SSPASEPSIC
TVAASTEQDG KADFSNFGQV VDVYAPGDSI TSAKPGGGSQ VLSGTSMATP HVAGLGAYLI
GLGKGGGPGL CDTIKQMAID VIQNPGASTT SKLINNGSGM