ID F6GSX9_VITVI Unreviewed; 452 AA.
AC F6GSX9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Serine/threonine-protein kinase AtPK2/AtPK19 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_17s0000g07520 {ECO:0000313|EMBL:CCB43020.1};
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:CCB43020.1, 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.
CC {ECO:0000256|RuleBase:RU000304}.
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DR EMBL; FN594950; CCB43020.1; -; Genomic_DNA.
DR RefSeq; XP_002280523.1; XM_002280487.4.
DR AlphaFoldDB; F6GSX9; -.
DR STRING; 29760.F6GSX9; -.
DR PaxDb; 29760-VIT_17s0000g07520-t01; -.
DR EnsemblPlants; Vitvi17g00727_t001; Vitvi17g00727_P001; Vitvi17g00727.
DR GeneID; 100244943; -.
DR Gramene; Vitvi17g00727_t001; Vitvi17g00727_P001; Vitvi17g00727.
DR KEGG; vvi:100244943; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_63_49_1; -.
DR InParanoid; F6GSX9; -.
DR OrthoDB; 5489497at2759; -.
DR Proteomes; UP000009183; Chromosome 17.
DR ExpressionAtlas; F6GSX9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 122..385
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 386..452
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 43..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 452 AA; 50058 MW; 6394D1580AAC8688 CRC64;
MIPSTPHKKT LHSILASKLK LTIPSPSSPD SLDFSDVFGP LTPHHHKASP SSSSPSSSSP
CVALGDPQVI HNRSHSLLGP SPRFAVTAPL LPFKEDMVFQ SEGSDKEGGD EVGEGRVGPG
DFEIMRVVGK GAFGKVFQVR KKGGPEISGD SDGIFAMKVM RKDTIISKNH MDYMKAERDI
LIKVEHPFIV SLRCSFQTNS KLYLIMDFVN GGHLFFHLYR QGIFSEDQAR VYIAEIVSAV
SHLHKSGIVH RDLKPENILM DADGHVMLTD FGLAKEIDES SRSNSMCGTT EYMAPEILLS
KGHNKDADWW SIGILLYEML TGQPPFTHAN RQKLQQRIIK EKVKLPSYLS SEAHSLLKGL
LQKEPSRRLG SGPTGGDEIQ NHKWFRSINW KKLEARELQP KFKPDVSGKD CTANFDQCWT
AMPLDDSPAP TPTAGGHFQG YTYVAPNPWL SS
//
