SUB2_TRIVC
ID SUB2_TRIVC Reviewed; 419 AA.
AC Q5VJ76;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Subtilisin-like protease 2;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB2;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS45674.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY439106; AAS45674.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q5VJ76; -.
DR SMR; Q5VJ76; -.
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_0000380774"
FT CHAIN 123..419
FT /note="Subtilisin-like protease 2"
FT /id="PRO_0000380775"
FT DOMAIN 36..122
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 131..419
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 419 AA; 45337 MW; 9FAA153582328845 CRC64;
MQLLNFGLLL LPFVAGDLAP QPEPLLAGPS DVVPGQYIVT LKEGLTSAQI RDHKKWVSSV
HRANLDSFAA GASGVETEGI MKHFHIHDLN MYSGGFDEKT VEDLSRNPYV KSVHPDQHVY
LAKTVTQRQA RWGLGYMSSK GKPVPLHSTL VDYSYDDKAG EGVWAYVLDT GINVNHIEFE
GRAILGHNAI PNKPHTDEFG HGTYVAGIIA GKTYGVAKKA NVVSAKAFDT GSSTYNYILE
TYDWIVRNIT DSNRKNKAVI NLSISGAKYQ PFDDAVEKAF KAGITTVVAA GNDGKDAKNN
TPASSPNAIT VGAVRWENTR PSFSNYGKLV DIWAPGELIK SCWKGGNNAT STQSGTSAAS
PHVAGLVAYL MSIENLPSPS AVTARVLNLT IPNLVKDAKD SPNRVAYNGI QERKFKLPK