ID   SUB7_TRITO              Reviewed;         401 AA.
AC   A1XIH4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Subtilisin-like protease 7;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB7;
OS   Trichophyton tonsurans (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=LAU 704;
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; DQ382273; ABD38559.1; -; Genomic_DNA.
DR   EMBL; FJ348241; ACL37331.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1XIH4; -.
DR   SMR; A1XIH4; -.
DR   VEuPathDB; FungiDB:TESG_06365; -.
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_0000380826"
FT   CHAIN           120..401
FT                   /note="Subtilisin-like protease 7"
FT                   /id="PRO_0000380827"
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;  41893 MW;  4BFF33C9DB3B6B66 CRC64;
     MGFITKAIPL ALAAASVING AEILETRAGV QTLADKYIVV MNDGMSDKDF DSHRSWVNRT
     HRRRLIRRGA KAMGGMKYTY NFPTGLKGYS GHFDEQMIKE ISKRADVKYI ERDARVQINA
     IEQQDNVPSW GLARVGSREP GGTTYYYDST AGEGTTAYII DTGTDIQHEE FDGGRATWGE
     NFVDDMDMDC NGHGTHVSGT VGGRTFGVAK KSNIVAVKVL DCNGSGSNSG VIMGMQWATE
     DAQSKGADKA VVNMSLGGAF SQTSNDAAKA IAEGGVFLAV AAGNDNVDAA EASPASEPSI
     CTVAASTEQD GKADFSNFGQ VVDVYAPGDG ITSAKPGGGS QVLSGTSMAS PHVAGLAAYL
     IGLGKGGGPQ LCDTIKQMAI DVIQNPGSST TSKLINNGSG M