ID D7SI39_VITVI Unreviewed; 731 AA.
AC D7SI39;
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=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
GN OrderedLocusNames=VIT_17s0000g06970 {ECO:0000313|EMBL:CBI15149.3};
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:CBI15149.3, 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000256|RuleBase:RU361128};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR EMBL; FN594950; CBI15149.3; -; Genomic_DNA.
DR RefSeq; XP_002281347.1; XM_002281311.3.
DR RefSeq; XP_010663284.1; XM_010664982.2.
DR AlphaFoldDB; D7SI39; -.
DR STRING; 29760.D7SI39; -.
DR PaxDb; 29760-VIT_17s0000g06970-t01; -.
DR EnsemblPlants; Vitvi17g00683_t001; Vitvi17g00683_P001; Vitvi17g00683.
DR GeneID; 100255335; -.
DR Gramene; Vitvi17g00683_t001; Vitvi17g00683_P001; Vitvi17g00683.
DR KEGG; vvi:100255335; -.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_003770_2_0_1; -.
DR InParanoid; D7SI39; -.
DR OMA; WQNEDDN; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000009183; Chromosome 17.
DR ExpressionAtlas; D7SI39; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd20805; C1_DGK_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..139
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 360..499
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 261..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 81008 MW; A6742E748F435A40 CRC64;
MDYYREPDVL LAWNNMSPSE MAESRLFIFS SLIAALVGIL TIAYTAFQWR RNINLSWMKA
MARSKKNPKT RDKVPVAPHT WILESVSRGK SLNCCVCLKS MSPSQTLGPM VASDSFIHRC
SICGAAAHLS CSSQAQKDCK CVSMKGYEHV IHQWAVQWTE ITDQLDETSF CSYCEEPCSG
SFLGGSPIWC CMWCQRLVHV DCHGIMSIET GDICDLGSFR RLILSPLFVK EVNRTSSGGF
LSSITHGANE IASSVRASIR NQGKKYKQGN EPSVDTTNSC DNGDISTEST AETHQTVNGS
HAMDEGCNGS TNIESPRQDS DVGKKLDSGS SFKRSASINQ KDESQVLQMK QRYELSDLPS
DARPLLVFIN KKSGSQRGGS LRQRLNILLN PVQVFELSSA QGPEVGLYLF KKVPHFRVLV
CGGDGTVGWV LNAIDKQNFV SPPPVAILPA GTGNDMARVL NWGGGLGSVE RQGGLCTVLH
HIEHAAVTML DRWKITILQQ GKQLQAPKFM NNYLGIGCDA KVALDIHNLR EENPEKFYNQ
FMNKVLYARE GAKNIMDRTF ADFPWQVRVE VDGVEVEVPE DAEGVLVANI GSYMGGVDLW
QNEDENYDNF DPQSMHDKML EVVSISGTWH LGKLQVGLSR ARRLAQGQSI KIHLFAPFPI
QIDGEPWFQE QLCTLTISHH GQAFMLKRVS EEPLGHAAAI ITDVLENAET NHIISASQKR
TLLQEMALKL S
//
