SUB4_TRIEQ
ID SUB4_TRIEQ Reviewed; 394 AA.
AC A7UKV6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Subtilisin-like protease 4;
DE EC=3.4.21.-;
DE Flags: Precursor; Fragment;
GN Name=SUB4;
OS Trichophyton equinum (Horse ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=63418;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Brown J.T., Preuett B.L., Abdel-Rahman S.M.;
RT "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT and Trichophyton equinum.";
RL Submitted (AUG-2007) 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; EU076571; ABU50381.1; -; Genomic_DNA.
DR AlphaFoldDB; A7UKV6; -.
DR SMR; A7UKV6; -.
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..17
FT /evidence="ECO:0000255"
FT PROPEP 18..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000380788"
FT CHAIN 117..>394
FT /note="Subtilisin-like protease 4"
FT /id="PRO_0000380789"
FT DOMAIN 36..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 126..394
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 100
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 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 394
SQ SEQUENCE 394 AA; 41614 MW; 1CCD1717DE699DC8 CRC64;
CLKTLSVFLA AFAAADARAV FKTQGHKNSE MIPDNYIVVM KDGVSQDDFK AHVSSVASIH
STNKAKRGTN TEGMKREFDI MNWRGYHGHF DRDTLEEILN DSKVDYVEQD QVVRISGLVT
QRGAPSWGLG RVSHRQAGSR DYVFDDSAGR GVTIYGVDTG IDINHQDFRG RARWGTNTAD
RDNADRHGHG THTASTFAGT AYGIAKNANI VAVKVLSSDG SGSTSGIIAG INYCVQDAQQ
RGILGKAAMN LSLGGGFSQA NNDAVTRAQN AGIFVAVAAG NDNRDARNYS PASAPAVCTV
ASSTINDSKS SFSNWGPVVD IYAPGSDIIA ARPGGGSTTM SGTSMASPHV AGMGAYMIGL
GADPRSLCDR LKQLATPAIR NPGSSTTNRL LYNG