ID D7SZI1_VITVI Unreviewed; 550 AA.
AC D7SZI1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Serine/threonine-protein kinase tricorner {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_05s0049g01220 {ECO:0000313|EMBL:CBI23658.3};
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:CBI23658.3, 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; FN595496; CBI23658.3; -; Genomic_DNA.
DR RefSeq; XP_010650104.1; XM_010651802.2.
DR RefSeq; XP_019075525.1; XM_019219980.1.
DR RefSeq; XP_019075526.1; XM_019219981.1.
DR AlphaFoldDB; D7SZI1; -.
DR STRING; 29760.D7SZI1; -.
DR PaxDb; 29760-VIT_05s0049g01220-t01; -.
DR EnsemblPlants; Vitvi05g00764_t001; Vitvi05g00764_P001; Vitvi05g00764.
DR GeneID; 100252887; -.
DR Gramene; Vitvi05g00764_t001; Vitvi05g00764_P001; Vitvi05g00764.
DR KEGG; vvi:100252887; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_0_1; -.
DR InParanoid; D7SZI1; -.
DR OMA; TQNFEQF; -.
DR OrthoDB; 988261at2759; -.
DR Proteomes; UP000009183; Chromosome 5.
DR ExpressionAtlas; D7SZI1; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21742; MobB_NDR_LATS-like; 1.
DR CDD; cd05599; STKc_NDR_like; 1.
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; PTHR24356:SF398; AGC (CAMP-DEPENDENT, CGMP-DEPENDENT AND PROTEIN KINASE C) KINASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 118..417
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 418..490
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 13..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..104
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 550 AA; 63280 MW; 3DBB1B6C4EC2D5C5 CRC64;
MKSIGCWFNK LKSRDKAKSS KKEATNNGKE GSKAVTSEEA PSNVTKQKVA AAKQYIENHY
KEQMKNLQER KERRNILEKK LADAEVSEEE QNNLLKHLEK KETEYMRLQR HKMGADDFEP
LTMIGKGAFG EVRVCREKKT GHVYAMKKLK KSEMLRRGQV EHVKAERNLL AEVDSNCIVK
LYCSFQDEEF LYLVMEYLPG GDMMTLLMRK DTLTEDEARF YVGETVLAIE SIHKHNYIHR
DIKPDNLLLD RYGHMKLSDF GLCKPLDCSN LHEKDFSLGN NLSGALQSDG RPAAPRRTQQ
EQLQHWQRNR RMLAYSTVGT PDYIAPEVLL KKGYGMECDW WSLGAIMYEM LVGYPPFYSD
EPMTTCRKIV NWRTHLKFPE EAKLSPEAKD LISKLLCNVD QRLGTKGADE IKAHPWFEGV
DWDKLYQIEA AFIPEVNDEL DTQNFEKFEE ADDQIQTSSK AGPWRKMLSS KDINFVGYTY
KNFEIVNDQP VPGIAELKKK STKTKRPSIK SLFDDESGAA ANEPVQGSFL NLLPPKLEVS
QKHGDPHRPH
//
