ID SUB3_TRIEQ Reviewed; 397 AA.
AC B6VA86;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Subtilisin-like protease 3;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB3;
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 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; FJ356724; ACJ04079.1; -; Genomic_DNA.
DR AlphaFoldDB; B6VA86; -.
DR SMR; B6VA86; -.
DR MEROPS; S08.115; -.
DR GlyCosmos; B6VA86; 2 sites, No reported glycans.
DR VEuPathDB; FungiDB:TEQG_06704; -.
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; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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 PANTHER; PTHR43806:SF68; ALKALINE PROTEASE 1; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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_0000380778"
FT CHAIN 117..397
FT /note="Subtilisin-like protease 3"
FT /id="PRO_0000380779"
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; 41230 MW; 838CEC3689FA899C CRC64;
MGCIKVISVF LAAIAAVDAR AFFHNRGGSD VIPNSYIVVM KDGVTTEDFD SHISTVAATH
NLNKAKRGSE TVGHKDSFNI NGWRAYNGHF DEATIESILN DDKVNYVEHD RVVKLAALVT
QPNAPTWGLG RVSHRAPGNR DFVYDSSAGQ GITIYGVDTG IDIRHPEFAG RIRWGTNTVD
NDNTDGNGHG THTAGTFAGT TYGVAKKANI VAVKVLSAGG SGSTAGVIKG IDWCVTDARS
RNALGKAALN LSLGGSFSQA NNDAVTRAQE AGIFVAVAAG NDNRDARNYS PASAPAVCTA
ASSTIDDQKS SFSNWGSIVD IYAPGSSILS AAPGGGTRTL SGTSMASPHV CGVGAAMLAQ
GVSVAQVCNR LKQIGNAVIR NPGTSTTNRL LYNGSGQ
//
