SUB6_TRIEQ
ID SUB6_TRIEQ Reviewed; 412 AA.
AC A1XIH0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Subtilisin-like protease 6;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB6;
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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=IHEM 15219;
RX PubMed=17156126; DOI=10.1111/j.1574-6968.2006.00541.x;
RA Giddey K., Favre B., Quadroni M., Monod M.;
RT "Closely related dermatophyte species produce different patterns of
RT secreted proteins.";
RL FEMS Microbiol. Lett. 267:95-101(2007).
RN [2]
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:0000269|PubMed:17156126}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; DQ382269; ABD38555.1; -; Genomic_DNA.
DR EMBL; FJ356726; ACJ04081.1; -; Genomic_DNA.
DR AlphaFoldDB; A1XIH0; -.
DR SMR; A1XIH0; -.
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 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW Virulence; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..126
FT /evidence="ECO:0000250"
FT /id="PRO_0000380808"
FT CHAIN 127..412
FT /note="Subtilisin-like protease 6"
FT /id="PRO_0000380809"
FT DOMAIN 36..120
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 135..412
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 358
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 412 AA; 42967 MW; 4AD43C36B50FDB4A CRC64;
MGFITKAIPI VLAALSTVNG AKILEAGPHA ETIPNKYIVV MKREVSDEAF SAHTTWLSQN
LNRRVMRRSG SSKAMAGMQD KYSLGGIFRA YSGEFDDAMI KDISSHDDVD YIEPDFVVRT
STNGTNLTRQ DNVPSWGLAR VSSKKAGGTT YYYDSSAGKG VTAYVIDTGI DINHEDFRGR
AKWGKNFVDD MDEDCNGHGT HVAGTVGGTK YGLAKGVSLV AVKVLDCEGS GSNSGVIKGM
EWAMREASGG GNGTAKAAGK AVMNMSLGGP RSQASNQAAK AISDAGIFMA VAAGNENMDA
QHSSPASEPS VCTVAASTED DGKADFSNYG QLVDVYAPGK DITSLKPGGS TDTLSGTSMA
SPHVCGLGAY LIGLGKQGGP GLCDTIKEMA HDAIQRPGEG TTSKLIYNGS GK