ID F6GZN7_VITVI Unreviewed; 765 AA.
AC F6GZN7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Subtilisin-like protease SBT1.7 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_18s0001g09360 {ECO:0000313|EMBL:CCB45769.1};
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:CCB45769.1, 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; FN595227; CCB45769.1; -; Genomic_DNA.
DR RefSeq; XP_002283279.2; XM_002283243.4.
DR AlphaFoldDB; F6GZN7; -.
DR MEROPS; S08.112; -.
DR PaxDb; 29760-VIT_18s0001g09360-t01; -.
DR EnsemblPlants; Vitvi18g00683_t001; Vitvi18g00683_P001; Vitvi18g00683.
DR GeneID; 100257444; -.
DR Gramene; Vitvi18g00683_t001; Vitvi18g00683_P001; Vitvi18g00683.
DR KEGG; vvi:100257444; -.
DR eggNOG; ENOG502QSVG; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; F6GZN7; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000009183; Chromosome 18.
DR ExpressionAtlas; F6GZN7; 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:SF388; XYLEM SERINE PROTEINASE 1; 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; 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..765
FT /note="Subtilisin-like protease SBT1.7"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003340502"
FT DOMAIN 31..106
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 130..601
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 369..456
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 656..761
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
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 211
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 541
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 765 AA; 80876 MW; 1C53CBD199D43DAA CRC64;
MKTWRLSIVV LVSFHFALVV AEEIKHQQKN TYIVHMDKSN MPTTFDDHFQ WYDSSLKTAS
SSADMLYTYN NVVHGFSTRL TTEEAELLRG QLGILSVLPE ARYELHTTRT PEFLGLGKSV
AFLPQADSAS EVIVGVLDTG VWPELKSFDD TGLGPVPSSW KGECETGKTF PLSSCNRKLI
GARFFSRGYE VAFGPVNETI ESRSPRDDDG HGSHTSTTAV GSAVEGASLF GFAAGTARGM
ATHARVAAYK VCWLGGCYGS DIVAAMDKAV QDGVDVLSMS IGGGLSDYTK DSVAIGAFRA
MEQGILVSCS AGNGGPAPSS LSNVAPWITT VGAGTLDRDF PAFVMLGDGK KFSGVSLYSG
KPLSDSLIPL VYAGNASSSP NGNLCIPDNL IPGKVAGKIV LCDRGSNARV QKGIVVKEAG
GVGMILTNTD LYGEELVADA HLLPTAAVGQ KAGDSIKSYI SSDPNPMATI APGGTQVGVQ
PSPVVASFSS RGPNPVTPEI LKPDIIAPGV NILAGWTGAV GPTGLQVDTR KVSFNIISGT
SMSCPHVSGL AALLKAAHPE WRPAAIKSAL MTTAYHTYKG GETIQDVATG RPATPFDYGA
GHVNPVSALD PGLVYDATVD DYLSFFCALN YKQDEIKRFT NRDFTCDMNK KYSVEDLNYP
SFAVPLQTAS GKGGGSGELT VVKYTRTLTN VGTPATYKVS VSSQISSVKI SVEPESLTFS
EPNEKKSYTV TFTASSMPSG MTSFAHLEWS DGKHIVGSPV AFSWT
//
