ID F6H4G6_VITVI Unreviewed; 714 AA.
AC F6H4G6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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_07s0031g02840 {ECO:0000313|EMBL:CCB47170.1};
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:CCB47170.1, 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 -!- 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; FN595233; CCB47170.1; -; Genomic_DNA.
DR RefSeq; XP_002272045.1; XM_002272009.3.
DR AlphaFoldDB; F6H4G6; -.
DR STRING; 29760.F6H4G6; -.
DR PaxDb; 29760-VIT_07s0031g02840-t01; -.
DR EnsemblPlants; Vitvi07g01961_t001; Vitvi07g01961_P001; Vitvi07g01961.
DR GeneID; 100247408; -.
DR Gramene; Vitvi07g01961_t001; Vitvi07g01961_P001; Vitvi07g01961.
DR KEGG; vvi:100247408; -.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_003770_2_0_1; -.
DR InParanoid; F6H4G6; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000009183; Chromosome 7.
DR ExpressionAtlas; F6H4G6; 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; IPR046349; C1-like_sf.
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:SF104; DIACYLGLYCEROL KINASE 2; 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; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
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|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 22..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..133
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 145..207
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 340..479
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 295..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 79809 MW; 917971E82BD00330 CRC64;
MIDLSNSLLR LLTTPDAYGP SVFGWLITGS FGILAIIYAF LKWQRRTSLN WIKAAAKAKK
KVWKRLNVPL SHHSWTEEFA YDVQPCTCSV CLTSLVSPQT LGAKATPQNP VHRCSVCGVA
AHFHCSKFAA KDCKCVAQAG FGHVQHQWSE RWIDMDDNHE MSAFCFYCDE PCGVPLLDAP
TWHCLWCQRL IHVKCHAKMS EESGDVCDLG ALRRLILSPI CVKEVDEEIT RSRMLSSITG
DIIASSVCGE IRRRRHRNKH GSVRSVNGKL QNTSPANTAL QYVLNGLASL KQSSNQNKDP
ILKRGGRVLS GKDTQNGWQK KGRSIPYGQV KKYTLVDLPQ DARPLLVFIN TKSGAQYGPS
LRRRLNMLLN PVQVFELSSS QGPEAGLNFF SNVQYFRVLV CGGDGTVAWV LDAIERHNFE
SPPPVAVLPL GTGNDLSRVL QWGRGFSTVN GQGGLSTLLA DINIAAVTML DRWEVNIQEE
RSDSDRCKVQ SKFMMNYLGI GCDAKVAYEF HTMREEKPEK FYSQFVNKLR YAKEGAKDIM
DRTCADLPWQ VWLEVDGRDI QIPKDAEGLI VLNIGSYMGG VDLWQNDYEH DDDFNLQCMH
DKMLEVVCIS GAWHLGKLQV GLSQARRVAQ GKVIRIHASS AFPVQIDGEP FIQQPGCLEI
THHGQVFMLR RASEEPRGHP AAIMTEVLVD AECRGVINAA QKKLLLQQMA LQLS
//
