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Database: UniProt
Entry: F6HGS6_VITVI
LinkDB: F6HGS6_VITVI
Original site: F6HGS6_VITVI 
ID   F6HGS6_VITVI            Unreviewed;       761 AA.
AC   F6HGS6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Subtilisin-like protease SBT1.8 {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=VIT_11s0016g00960 {ECO:0000313|EMBL:CCB51390.1};
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:CCB51390.1, 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; FN595756; CCB51390.1; -; Genomic_DNA.
DR   RefSeq; XP_002278292.1; XM_002278256.3.
DR   AlphaFoldDB; F6HGS6; -.
DR   STRING; 29760.F6HGS6; -.
DR   MEROPS; S08.A24; -.
DR   PaxDb; 29760-VIT_11s0016g00960-t01; -.
DR   EnsemblPlants; Vitvi11g00071_t001; Vitvi11g00071_P001; Vitvi11g00071.
DR   GeneID; 100264662; -.
DR   Gramene; Vitvi11g00071_t001; Vitvi11g00071_P001; Vitvi11g00071.
DR   KEGG; vvi:100264662; -.
DR   eggNOG; ENOG502QRTY; Eukaryota.
DR   HOGENOM; CLU_000625_4_6_1; -.
DR   InParanoid; F6HGS6; -.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000009183; Chromosome 11.
DR   ExpressionAtlas; F6HGS6; baseline and differential.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
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:SF335; SUBTILISIN-LIKE PROTEASE SBT1.8; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..761
FT                   /note="Subtilisin-like protease SBT1.8"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003335799"
FT   DOMAIN          24..100
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          130..581
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          372..454
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          655..755
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   REGION          196..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        540
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   761 AA;  81102 MW;  D04112A4579B9E9A CRC64;
     MASVVWLFSF WFACFSLSVM AKRTYIVQMN HRQKPLSYAT HDDWYSASLQ SISSNSDDLL
     YTYSTAYHGF AASLDPEQAE ALRKSDSVMG VYEDEVYSLH TTRSPEFLGL DTELGLWAGH
     RTQDLNQASQ DVIIGVLDTG VWPDSRSFDD SGMTEVPARW RGKCEEGPDF QASSCNKKLI
     GAQSFSKGYR MASGGNFVKK SKEKESPRDV DGHGTHTAST AAGAHVSNAS LLGYASGTAR
     GMATHARVAA YKVCWSTGCF GSDILAGMDR AIVDGVDVLS LSLGGGSGPY YRDTIAIGAF
     TAMEMGIFVS CSAGNSGPSK ASLANVAPWI MTVGAGTLDR DFPAYALLGN GKKITGVSLY
     SGRGMGKKPV SLVYSKGNST SNLCLPGSLQ PAYVRGKVVI CDRGINARVE KGLVVRDAGG
     VGMILANTAV SGEELVADSH LLPAVAVGRK VGDVLRAYVK SVANPTALLS FGGTVLNVRP
     SPVVAAFSSR GPNLVTPQIL KPDLIGPGVN ILAAWSEALG PTGLEKDTRK TQFNIMSGTS
     MSCPHISGVA ALIKAAHPEW SPSAVKSALM TTAYTRDNTK SPLRDAADGG LSTPLAHGSG
     HVDPQKALSP GLVYDISTQD YVAFLCSLDY TIEHVRAIVK RQNITCSRKF SDPGELNYPS
     FSVLFGSKGF VRYTRELTNV GAADSVYQVA VTGPPSVGVV VRPSTLVFKN VGEKKRYTVT
     FVAKKGKKVQ NRMTRSAFGS IVWSNTQHQV KSPVAYAWTQ L
//
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