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Database: UniProt
Entry: D7TVU0_VITVI
LinkDB: D7TVU0_VITVI
Original site: D7TVU0_VITVI 
ID   D7TVU0_VITVI            Unreviewed;       737 AA.
AC   D7TVU0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Subtilisin-like protease SBT3.6 {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=VIT_02s0025g02880 {ECO:0000313|EMBL:CBI34615.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI34615.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; FN596251; CBI34615.3; -; Genomic_DNA.
DR   AlphaFoldDB; D7TVU0; -.
DR   MEROPS; S08.A22; -.
DR   PaxDb; 29760-VIT_02s0025g02880-t01; -.
DR   EnsemblPlants; Vitvi02g00260_t001; Vitvi02g00260_P001; Vitvi02g00260.
DR   Gramene; Vitvi02g00260_t001; Vitvi02g00260_P001; Vitvi02g00260.
DR   eggNOG; ENOG502QSF0; Eukaryota.
DR   HOGENOM; CLU_000625_4_2_1; -.
DR   InParanoid; D7TVU0; -.
DR   OMA; NGIMPCA; -.
DR   Proteomes; UP000009183; Chromosome 2.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02120; PA_subtilisin_like; 1.
DR   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 2.60.40.2310; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; IPR034197; Peptidases_S8_3.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF737; SUBTILISIN-LIKE PROTEASE SBT3.5 ISOFORM X1; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          3..75
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          100..554
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          631..726
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        185
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        516
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   737 AA;  79330 MW;  57351A68339B1183 CRC64;
     MGEKKHEDPA TIKKCHHEML STLLGSKEAA KSSILYSYKH GFSGFAAKLT ESQAEDIAGF
     PGVVQVIPNR IHRLHTTRSW DFLGLQHDYP TNVLTETNLG RGVIIGVIDS GVWPESESFK
     DEGMGPIPSR WKGICQHGER FNSTNCNRKL IGARWFFKGI HQEIGKFMNI TDNLEFLSPR
     DGIGHGTHTA STAAGYFVEK ANYRGLATGL ARGGAPLARL AIYKACWAII SGACSDADIL
     KAFDKAIHDG VDILSLSVGN DIPLFSYVDQ RDSIAIASFH AIAKGITVVC SAGNDGPFSQ
     TIANTAPWLI TVAATTIDRA FPTAIILGNN QTFLGQSIDT GKHKLGFTGL TYSERVALDP
     KDDSAKDCQP GSLNATLAAG KIILCFSKSD KQDIISASGA VLEAGGIGLI FAQFPTSQLE
     SCDLIPCIKV NYEVGTQILT YIRKARSPTA KLKFPKTVTG KWASPHVAYF SSRGPSSMSP
     AVLKPDVAAP GVNILAAYSP VDAGTSNGFA FLSGTSMACP HVSGLAALIK SAHPTWSPAA
     IRSALVTSAS QTGTDGMDII EEGPTRKAAD PFDIGGGHVN PNKALKPGLI YNISMEDYIQ
     FLCSMGYSNP SIGRLTKTTT NCTRGSHFQL NLNLPSITIP NLKKKVTVMR TVTNVGHINS
     VYKAEVQAPY GIKMAVEPHI LSFNLTTQFL HFKVTFFSTQ TVHGDYKFGS LTWTDGEHFV
     RSPIAIRAIK FDMYADV
//
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