SUB3_TRIVH
ID SUB3_TRIVH Reviewed; 397 AA.
AC D4DLA2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Subtilisin-like protease 3;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB3; ORFNames=TRV_07976;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACYE01000498; EFE37368.1; -; Genomic_DNA.
DR RefSeq; XP_003018013.1; XM_003017967.1.
DR AlphaFoldDB; D4DLA2; -.
DR SMR; D4DLA2; -.
DR EnsemblFungi; EFE37368; EFE37368; TRV_07976.
DR GeneID; 9579144; -.
DR KEGG; tve:TRV_07976; -.
DR HOGENOM; CLU_011263_1_3_1; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000397788"
FT CHAIN 117..397
FT /note="Subtilisin-like protease 3"
FT /id="PRO_0000397789"
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; 41015 MW; DF226D3E55028608 CRC64;
MGCIKVISVF LAAIAAVDAR AFFHNRGGND VIPNSYIVVM KDGVTAEDFD SHISSVAATH
SLNKAKRGSE TVGHKDSFNI NGWRAYNGHF DEATIESILK DDKVNYVEHD RVVKLAALTT
QPNAPTWGLG RVSHKAPGNK DFVYDSSAGQ GITIYGVDTG IDIRHPEFAG RIRWGTNTVD
NDNTDGNGHG THTAGTFAGT TYGVAKKANI VAVKVLSAGG SGSTSGVIKG IDWCVTDARS
KNALGKAALN LSLGGSFSQA SNDAVTRAQE AGIFVAVAAG NDNRDAKNSS PASAPAVCTA
ASSTIDDQKS SFSNWGTIVD IYAPGSNILS AAPGGGTRTL SGTSMASPHV CGVGAAMLAQ
GVSVAQACDR LKQIGNAVIR NPGTGTTNRL LYNGSGR