ID F6HZG8_VITVI Unreviewed; 1111 AA.
AC F6HZG8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN OrderedLocusNames=VIT_07s0005g02790 {ECO:0000313|EMBL:CCB60083.1};
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:CCB60083.1, 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 protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; FN596502; CCB60083.1; -; Genomic_DNA.
DR RefSeq; XP_010652346.1; XM_010654044.2.
DR RefSeq; XP_010652347.1; XM_010654045.2.
DR AlphaFoldDB; F6HZG8; -.
DR PaxDb; 29760-VIT_07s0005g02790-t01; -.
DR EnsemblPlants; Vitvi07g00543_t001; Vitvi07g00543_P001; Vitvi07g00543.
DR GeneID; 104879811; -.
DR Gramene; Vitvi07g00543_t001; Vitvi07g00543_P001; Vitvi07g00543.
DR KEGG; vvi:104879811; -.
DR eggNOG; ENOG502QSHG; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; F6HZG8; -.
DR OrthoDB; 449350at2759; -.
DR Proteomes; UP000009183; Chromosome 7.
DR ExpressionAtlas; F6HZG8; baseline and differential.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 6.
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; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48054:SF52; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE RPK2; 1.
DR PANTHER; PTHR48054; RECEPTOR KINASE-LIKE PROTEIN XA21; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1111
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003341747"
FT TRANSMEM 769..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 832..1106
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 725..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 860
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1111 AA; 121601 MW; 745E919F388E8353 CRC64;
MATKLRRHRP TAHRRFLCFS LVVVLGICWA VAMEGTSLSS YSSSSWDDKL TLLELKSCVT
QDPLGFLTNW NPNDPDPCSW NGVICDTLSR RVTALDLSSN RNCSFLSLFA TPASDVHAAC
LLGGGFNKSS SSASKLRGRL PPIVGRLSQL RVLSLGFNGF FGEVPREIGH LALLEVLDVA
SNAFHGPIPP ALRNCTALRV VNLSGNRFNG TIPELLADLP SLQILSLSYN MLSGVIPEEL
GHNCGTLEHL YLTGNSLSGS IPASLGNCSM LRSLFLSSNK FENEIPSSFG KLGMLEALDL
SRNFLSGIIP SQLGNCTQLK LLVLKNNFGP LLLWRNEEVE DYNYFVGQLP NSIVKLPNLH
VFWAPQANLE GIFPQNWGSC SNLEMLNLAQ NYFTGQIPTS LGKCKSLYFL DLNSNNLTGF
LPKEISVPCM VVFNISGNSL SGDIPRFSQS ECTEKVGNPW MSDIDLLGLY SSFFYWNAVT
SIAYFSSPSY GLVMLHDFSN NLFTGLVPPL LITSDRLSVR PSYGFWVEGN NLKGNTSTLS
FDSCQSLNSL VFDIASNKIT GELPPKLGSC KYMKLLNVAG NELVGSIPLS FANLSSLVNL
NLSGNRLQGP IPSYIGKMKN LKYLSLSGNN FSGTIPLELS QLTSLVVLEL SSNSLSGQIP
SDFAKLEHLD IMLLDHNHLS GKIPSSFGNL TSLSVLNVSF NNLSGSFPLN SNWVKCENVQ
GNPNLQPCYD DSSSTEWERR HSDDVSQQEA YPPTGSRSRK SDVFSPIEIA SITSASIIVF
VLIALVLLYV SMKKFVCHTV LGQGSGKKEV VTCNNIGVQL TYENVVRATG SFNVQNCIGS
GGFGATYKAE IVPGVVVAVK RLSVGRFQGV QQFAAEIRTL GRVQHPNLVT LIGYHVSEAE
MFLIYNYLPG GNLEKFIQDR TRRTVEWSML HKIALDIARA LAYLHDECVP RVLHRDIKPS
NILLDNNFNA YLSDFGLARL LGTSETHATT DVAGTFGYVA PEYAMTCRVS DKADVYSYGV
VLLELISDKK ALDPSFSSFG NGFNIVAWAS MLLRQGQACD FFTAGLWESG PHDDLIEILH
LAIMCTGESL STRPSMKQVA QRLKRIQPPT C
//
