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Database: UniProt
Entry: F6H5Q7_VITVI
LinkDB: F6H5Q7_VITVI
Original site: F6H5Q7_VITVI 
ID   F6H5Q7_VITVI            Unreviewed;       878 AA.
AC   F6H5Q7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   OrderedLocusNames=VIT_14s0108g00340 {ECO:0000313|EMBL:CCB47528.1};
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:CCB47528.1, 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).
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DR   EMBL; FN595239; CCB47528.1; -; Genomic_DNA.
DR   RefSeq; XP_002277606.1; XM_002277570.3.
DR   AlphaFoldDB; F6H5Q7; -.
DR   PaxDb; 29760-VIT_14s0108g00340-t01; -.
DR   EnsemblPlants; Vitvi14g03074_t001; Vitvi14g03074_P001; Vitvi14g03074.
DR   GeneID; 100268107; -.
DR   Gramene; Vitvi14g03074_t001; Vitvi14g03074_P001; Vitvi14g03074.
DR   KEGG; vvi:100268107; -.
DR   eggNOG; ENOG502QVKB; Eukaryota.
DR   HOGENOM; CLU_000288_22_1_1; -.
DR   InParanoid; F6H5Q7; -.
DR   OrthoDB; 1128609at2759; -.
DR   Proteomes; UP000009183; Chromosome 14.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR   PANTHER; PTHR48005:SF16; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 6.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00365; LRR_SD22; 7.
DR   SMART; SM00369; LRR_TYP; 11.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        522..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          588..861
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         616
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   878 AA;  96903 MW;  D5CC7F7DFC64AE5B CRC64;
     MASSIIISPA VVVVTITSIM MIMLFSLANA LSSPSSSTDE AEALRSTGWW NSTSAHCNWD
     GVYCNNAGRV TQIAFFDSGK KLGELSKLEF SSFPSLVELF LSDCGLNGSI PHQIGTLTQL
     IILYLPLNNL TGELPLSLAN LTQLEYLSLH SNRLHGSIPP EIGKMKNLIY FILHDNNLTG
     VIPSSFGNLT NLTYLYLGSN QISGFIPPQI GKMKNLEFLS LSYNGLHGSI PPEIGKLQNL
     NYLFLDYNNL TSVIPSSFGN LTNLTYLYLD SNQISGFIPP QIGKIKNLEL LELSYNGLHG
     PIPLEIGKLK NLKILNLGYN NLIGVIPSSF GNLTNLTYLT LGGNQISGFI PPEIGKMKNL
     IFFNLGYNSL TGVIPSSFGN LTHLTSLILR GNQINGSIPP EIGYLLDLLY LDLNTNQISG
     FIPEEILNLK KLGHLDISNN LISGKIPSEL GNLKEAIYFN LSRNNISGTI PLSISNNMWT
     LFDLSHNQLE GQSTAPLEAF DHNKGLCDGI KGLSHCKKRH QIILIIAISL SATLLLSVAV
     LGFLFRKQKI RKNQLPKTTK VKNGDLFSIW DYDGVIAYQD IIQATEDFDI KYCIGTGGYG
     SVYRAQLPSG KVVALKKLHG WERDDPTYLK SFENEVQMLS RIQHRNIVKL HGFCLHNKCM
     FLVYKYMEKG SLYCMLRDEV EVVQLDWIKR VNVVKGIANA LSYMHHDSTL PIIHRDISSN
     NILLDSKLEA FVADFGTARL LDPDSSNQTL LAGTYGYIAP ELAYTMVVTE KCDVYSFGMV
     ALETIMGKHP GDLVTSLSAS STQNITLKDV LDSRLSSPKG PQVANDVALV VSLALKCLHC
     NPRFRPSMQQ VSWRLSASKS FPQPVGAISL LQLKNEEI
//
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