SUB7_TRIEQ
ID SUB7_TRIEQ Reviewed; 401 AA.
AC A1XIH3; A7UKV7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Subtilisin-like protease 7;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=SUB7;
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] OF 1-339.
RA Brown J.T., Preuett B.L., Abdel-Rahman S.M.;
RT "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT and Trichophyton equinum.";
RL Submitted (AUG-2007) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABU50382.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ382272; ABD38558.1; -; Genomic_DNA.
DR EMBL; EU076572; ABU50382.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A1XIH3; -.
DR SMR; A1XIH3; -.
DR MEROPS; S08.061; -.
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_0000380820"
FT CHAIN 120..401
FT /note="Subtilisin-like protease 7"
FT /id="PRO_0000380821"
FT DOMAIN 36..118
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 129..401
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 193
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 347
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 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 401 AA; 41865 MW; C424CBA03BC30A1F CRC64;
MGFITKAIPL ALAAASVING AEILETRAGV QTLADKYIVV MNDGMSDKDF DSHRSWVNRT
HRRRLIRRGA KAMGGMKYTY NFPTGLKGYS GHFDEQMIKE ISKRADVKYI ERDARVQINA
IEQQDNVPSW GLARVGSREP GGTTYYYDST AGEGTTAYII DTGTDIQHEE FDGGRATWGE
NFADDMDMDC NGHGTHVSGT VGGRTFGVAK KSNIVAVKVL DCNGSGSNSG VIMGMQWATE
DAQSKGADKA VVNMSLGGAF SQTSNDAAKA IAEGGVFLAV AAGNDNVDAA EASPASEPSI
CTVAASTEQD GKADFSNFGQ VVDVYAPGDG ITSAKPGGGS QVLSGTSMAS PHVAGLAAYL
IGLGKGGGPQ LCDTIKQMAI DVIQNPGSST TSKLINNGSG M