SUB2_TRIEQ
ID SUB2_TRIEQ Reviewed; 421 AA.
AC B6VA85;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Subtilisin-like protease 2;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB2;
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; FJ356723; ACJ04078.1; -; Genomic_DNA.
DR AlphaFoldDB; B6VA85; -.
DR SMR; B6VA85; -.
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; IPR023827; Peptidase_S8_Asp-AS.
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; PS00136; SUBTILASE_ASP; 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..16
FT /evidence="ECO:0000255"
FT PROPEP 17..122
FT /evidence="ECO:0000250"
FT /id="PRO_0000380768"
FT CHAIN 123..421
FT /note="Subtilisin-like protease 2"
FT /id="PRO_0000380769"
FT DOMAIN 36..122
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 131..421
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 357
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 421 AA; 45576 MW; 76BADB28ACACB4F6 CRC64;
MQLLNFGLLL LPFVAGDLAP QPEPLLAGPS DVVPGQYIVT LKEGLTSAQI RDHKKWVSSV
HRANLEGFAA GASGVETEGI MKHFHIHDLN MYSGGFDEKT VEDLSRNPYV KSVHPDQHVY
LAKTVTQRQA RWGLGYMSSK GKPVPLHSTL VDYSYDDKAG EGVWAYVLDT GINVNHVEFE
GRAILGHNAI PNKPHTDEFG HGTYVAGIIA GKTYGVAKKA NVVSAKAFDT GSSTYNYILE
TYDWIVRNIT DSNRKNKAVI NLSISGAKYQ PFDDAVEKAF KAGIATVVAA GNDGKDAKNN
TPASSPNAIT VGAVRWENTR PSFSNYGKIV DIWAPGELIK SCWKGGNNAT STQSGTSAAS
PHVAGLVAYL MSTENLPSPS AVTARVLNLT IPNLVKDAKD SPNRVVYNGI QERKFTLPKY
F
