ID   SUB7_ARTBC              Reviewed;         420 AA.
AC   D4APA9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Subtilisin-like protease 7;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB7; ORFNames=ARB_06076;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   INDUCTION.
RX   PubMed=19942661; DOI=10.1099/mic.0.033464-0;
RA   Staib P., Zaugg C., Mignon B., Weber J., Grumbt M., Pradervand S.,
RA   Harshman K., Monod M.;
RT   "Differential gene expression in the pathogenic dermatophyte Arthroderma
RT   benhamiae in vitro versus during infection.";
RL   Microbiology 156:884-895(2010).
CC   -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC       activity that contributes to pathogenicity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460}.
CC   -!- INDUCTION: Expression is up-regulated during infection.
CC       {ECO:0000269|PubMed:19942661}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE35120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000004; EFE35120.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003015765.1; XM_003015719.1.
DR   AlphaFoldDB; D4APA9; -.
DR   SMR; D4APA9; -.
DR   STRING; 63400.XP_003015765.1; -.
DR   EnsemblFungi; EFE35120; EFE35120; ARB_06076.
DR   GeneID; 9526046; -.
DR   KEGG; abe:ARB_06076; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_011263_1_3_1; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
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; Reference proteome; Secreted;
KW   Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..119
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397804"
FT   CHAIN           120..420
FT                   /note="Subtilisin-like protease 7"
FT                   /id="PRO_0000397805"
FT   DOMAIN          36..118
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          129..413
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   420 AA;  43992 MW;  36AE8C2C40B0C0F7 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 SKLINNGSGI GFLSFPLNIY EEQWSKLFDL