SUB4_TRITO
ID SUB4_TRITO Reviewed; 399 AA.
AC B8XGQ7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Subtilisin-like protease 4;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB4;
OS Trichophyton tonsurans (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=34387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Preuett B.L., Abdel-Rahman S.M.;
RT "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT and Trichophyton equinum.";
RL Submitted (OCT-2008) 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; FJ348239; ACL37329.1; -; Genomic_DNA.
DR AlphaFoldDB; B8XGQ7; -.
DR SMR; B8XGQ7; -.
DR MEROPS; S08.115; -.
DR VEuPathDB; FungiDB:TESG_04167; -.
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..118
FT /evidence="ECO:0000250"
FT /id="PRO_0000380792"
FT CHAIN 119..399
FT /note="Subtilisin-like protease 4"
FT /id="PRO_0000380793"
FT DOMAIN 38..117
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 128..399
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 191
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 102
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 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 399 AA; 42087 MW; 3DC5A22E9AB9299C CRC64;
MVCLKTLSVF LAAFAAADAR AVFKTQGHKN SEMIPDNYIV VMKDGVSQDD FKAHVSSVAS
IHSTNKAKRG TNTEGMKREF DIMNWRGYHG HFDRDTLEEI LNDSKVDYVE QDQVVRISGL
VTQRGAPSWG LGRVSHRQAG SRDYVFDDSA GRGVTIYGVD TGIDINHQDF RGRARWGTNT
ADRDNADRHG HGTHTASTFA GTAYGIAKNA NIVAVKVLGS DGSGSTSGII AGINYCVQDA
QQRGILGKAA MNLSLGGGFS QANNDAVTRA QNAGIFVAVA AGNDNRDARN YSPASAPAVC
TVASSTINDS KSSFSNWGPV VDIYAPGSDI IAARPGGGST TMSGTSMASP HVAGMGAYMI
GLGADPRSLC DRLKQLATPA IRNPGSSTTN RLLYNGSGQ
