SUB7_TRISD
ID SUB7_TRISD Reviewed; 400 AA.
AC A1XIH5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Subtilisin-like protease 7;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB7;
OS Trichophyton soudanense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=69891;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=LAU 228;
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).
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; DQ382274; ABD38560.1; -; Genomic_DNA.
DR AlphaFoldDB; A1XIH5; -.
DR SMR; A1XIH5; -.
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; IPR022398; Peptidase_S8_His-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; PS00137; SUBTILASE_HIS; 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..119
FT /evidence="ECO:0000250"
FT /id="PRO_0000380822"
FT CHAIN 120..400
FT /note="Subtilisin-like protease 7"
FT /id="PRO_0000380823"
FT DOMAIN 36..118
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 129..400
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 222
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 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 400 AA; 41588 MW; 2DEC32799CF2CC9A CRC64;
MGFITKAIPL ALAAASVING AEILETRAGV QTLADKYIVV MNDGISDKDF DSHRSWVNRN
HRRRLIRRGA KAMGGMKHTY NFPTGLKGYS GHFDEQMINE ISKRADVKYI ERDARVQINA
IEQQDNVPSW GLARVGSKEP GGTTYYYDST AGEGSTAYVI DTGTDIQHEE FEGRATWGAN
FVDDMDMDCN GHGTHVSGTI GGKTFGVAKK SNVVAVKVLD CNGSGSNSGV IMGMEWATKD
AQQKGADKAV ANMSLGGAFS QASNDAAAAI AKGGVFLAVA AGNDNVDAAD SSPASEPSIC
TIAASTEQDS KADFSNFGQV VDVYAPGDSI TSAKPGGGSQ VLSGISMATP HVAGLGAYLI
GLGKGGGPGL CDTIKQMAID VIQNPGASTT SKLINNGSGM
