SUB3_TRIVC
ID SUB3_TRIVC Reviewed; 397 AA.
AC Q5VJ75;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Subtilisin-like protease 3;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB3;
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; AY439107; AAS45675.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5VJ75; -.
DR SMR; Q5VJ75; -.
DR MEROPS; S08.115; -.
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; Secreted; Serine protease; Signal;
KW Virulence; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000380784"
FT CHAIN 117..397
FT /note="Subtilisin-like protease 3"
FT /id="PRO_0000380785"
FT DOMAIN 35..116
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 126..397
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 344
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 41015 MW; DF226D3E55028608 CRC64;
MGCIKVISVF LAAIAAVDAR AFFHNRGGND VIPNSYIVVM KDGVTAEDFD SHISSVAATH
SLNKAKRGSE TVGHKDSFNI NGWRAYNGHF DEATIESILK DDKVNYVEHD RVVKLAALTT
QPNAPTWGLG RVSHKAPGNK DFVYDSSAGQ GITIYGVDTG IDIRHPEFAG RIRWGTNTVD
NDNTDGNGHG THTAGTFAGT TYGVAKKANI VAVKVLSAGG SGSTSGVIKG IDWCVTDARS
KNALGKAALN LSLGGSFSQA SNDAVTRAQE AGIFVAVAAG NDNRDAKNSS PASAPAVCTA
ASSTIDDQKS SFSNWGTIVD IYAPGSNILS AAPGGGTRTL SGTSMASPHV CGVGAAMLAQ
GVSVAQACDR LKQIGNAVIR NPGTGTTNRL LYNGSGR
