SUB5_TRIVC
ID SUB5_TRIVC Reviewed; 396 AA.
AC Q5VJ73;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Subtilisin-like protease 5;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB5;
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}.
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DR EMBL; AY439109; AAS45677.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5VJ73; -.
DR SMR; Q5VJ73; -.
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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000380804"
FT CHAIN 117..396
FT /note="Subtilisin-like protease 5"
FT /id="PRO_0000380805"
FT DOMAIN 37..113
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 125..396
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 376..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 396 AA; 41763 MW; 5102577CB2815B97 CRC64;
MTGFFTILSF SLAALSVTNA AQILSVPKGA EVVPNGYIVV MKDDTSQQDF SSHRVWISSI
HHNMTRRGLD GAGVKQTYDF DHLRGYSGIF DEDTIKDISN DPKVAFVEPD AIISQHVVVQ
QRKAPWGLSR LSNRRGGRNY VFDSSAGSGV WAYVVDSGVD VRHAEFQGRA VWGSNLVDNK
NSDGTGHGTH VAGTIAGKTY GIAKKAKVVA VKVLNSEGKG PTSGIIAGIN WSIRHARKHG
MLQKSVLNMS LGGTYSAGLN HATAQAIKAG MFVSVSAGND NINSNGNSPA SERSVCTIAA
STENDGKASF SNWGPAVDLY APGHNILSAR PGGGSQTMSG TSMAAPHAAG VAAYLIAKEG
IPGNRACLRL KQLSQPTIRN PGPDTTSRLL YNGSGR
