SUB1_TRIVC
ID SUB1_TRIVC Reviewed; 399 AA.
AC Q5VJ77;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Subtilisin-like protease 1;
DE EC=3.4.21.-;
DE Flags: Precursor; Fragment;
GN Name=SUB1;
OS Trichophyton verrucosum (Cattle ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=63417;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jousson O., Monod M.;
RT "Subtilisin-like proteases gene family in Dermatophytes.";
RL Submitted (OCT-2003) 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:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AY439105; AAS45673.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5VJ77; -.
DR SMR; Q5VJ77; -.
DR MEROPS; S08.025; -.
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; 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; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW Virulence; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000380763"
FT CHAIN 117..>399
FT /note="Subtilisin-like protease 1"
FT /id="PRO_0000380764"
FT DOMAIN 34..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 126..399
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 175..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 399
SQ SEQUENCE 399 AA; 41427 MW; E0D2968780B2332E CRC64;
MGVFRFISIS LAAVSAANAA QILSMPHAQT VPNSYIVMMK DDTSDDDFNH HQSWLQSTHT
HNITRRATIQ NAGMRHKYNF SKMKGYSGIF DEETIKDIAK DPKVMFVEPD TIISVHGKVE
QSNVPSWGLA RISNPQPGAG SYIYDSSAGE GITVYSVDTG VDVNHEDFEG RAIWGSNQVN
DGDDRDGSGH GTHTSGTMVG KEFGIAKKAK LVAVKVLGND GSGPTSGIVA GINWSVEHAR
QNGGTKKAVM NMSLGGSSSS ALNRAAAQAV EQGMFLSVAA GNDNQDAQSS SPASEPSVCT
VGSSAEDDSR SSFSNWGPAI DLFAPGSNII SARPGGGSQS MSGTSMAAPH VAGLAAYLMA
LEGISGGAVC DRLKELGTSS ITDAGPGTPT NVLINNGGA