ID Q8J1M1_ARTBE Unreviewed; 292 AA.
AC Q8J1M1;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Subtilisin-like protease 6 {ECO:0000256|ARBA:ARBA00044136};
DE Flags: Fragment;
GN Name=tri m 2 {ECO:0000313|EMBL:CAD23613.1};
OS Arthroderma benhamiae (Trichophyton mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=63400 {ECO:0000313|EMBL:CAD23613.1};
RN [1] {ECO:0000313|EMBL:CAD23613.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 432.54 {ECO:0000313|EMBL:CAD23613.1};
RA Probst S., Polyakov I., Ivanova L., Graeser Y.;
RT "Development of DNA markers to explore the genetic relatedness of strains
RT of the two dermatophyte species causing Favus of human and mouse.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AJ430838; CAD23613.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8J1M1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF69; PROTEINASE T; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Virulence {ECO:0000256|ARBA:ARBA00023026};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 54..268
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 63
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 94
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 254
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAD23613.1"
FT NON_TER 292
FT /evidence="ECO:0000313|EMBL:CAD23613.1"
SQ SEQUENCE 292 AA; 29874 MW; 73D67395B13F70D4 CRC64;
NHDDVDYIEP DFVVRTSTNG TNLTRQENVP SWGLARVGSK KAGGTTYYYD SSAGKGVTAY
IIDTGIDINH EDFGGRAKWG KNFVDKMDED CNGHGTHVAG TVGGTKYGLA KGVTLVAVKV
LDCDGSGSNS GVIEGMEWAM REASGGGNGT AKAAGKAVMN MSLGGPRSQA SNDAAKAISD
AGIFMAVAAG NENMDAQHSS PASEPSVCTV AASTEDDGKA EFSNYGAVVD VYAPGKDITS
LKPGGSTDTL SGTSMASPHV CGLGAYLIGL GKQGGPGLCD TIKEMANEAI QR
//
