SUB7_ARTBE
ID SUB7_ARTBE Reviewed; 400 AA.
AC Q64K36;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Subtilisin-like protease 7;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB7;
OS Arthroderma benhamiae (Trichophyton mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=63400;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15363848; DOI=10.1016/j.gene.2004.06.024;
RA Jousson O., Lechenne B., Bontems O., Mignon B., Reichard U., Barblan J.,
RA Quadroni M., Monod M.;
RT "Secreted subtilisin gene family in Trichophyton rubrum.";
RL Gene 339:79-88(2004).
CC -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC activity that contributes to pathogenicity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15363848}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AY437852; AAS45666.1; -; Genomic_DNA.
DR AlphaFoldDB; Q64K36; -.
DR SMR; Q64K36; -.
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; 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; 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..119
FT /evidence="ECO:0000250"
FT /id="PRO_0000380818"
FT CHAIN 120..400
FT /note="Subtilisin-like protease 7"
FT /id="PRO_0000380819"
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 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 41581 MW; 1DE26BE928AEE6D9 CRC64;
MGFITKAIPL ALAAASVING AEIMETRAGV QTLADKYIVV MNDGMTDKDF DSHRSWVNRT
HRRRLIRRGA KAMGGMKHTY RFPTGLKGYS GHFDEQMINE ISKRADVKYI ERDARVQINA
IEQQDNVPSW GLARVGSKEP GGTTYYYDGT AGEGSTAYVI DTGTDIQHEE FEGRATWGAN
FVDDMDMDCN GHGTHVSGTI GGKTFGVAKK SNVVAVKVLD CNGSGSNSGV IMGMEWATKD
AQQKGADKAV ANMSLGGAFS QASNDAAAAI AKGGVFLAVA AGNDNVDAAD SSPASEPSIC
TVAASTEQDS KADFSNFGQV VDVYAPGDSI TSAKPGGGSQ VLSGTSMATP HVAGLGAYLI
GLGKGGGPGL CDTIKQTAID VIQNPGASTT SKLINNGSGM
