ID A0A0Q3I5D8_BRADI Unreviewed; 530 AA.
AC A0A0Q3I5D8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Diacylglycerol kinase {ECO:0000256|PIRNR:PIRNR030829, ECO:0000256|RuleBase:RU361128};
DE EC=2.7.1.107 {ECO:0000256|PIRNR:PIRNR030829, ECO:0000256|RuleBase:RU361128};
GN Name=100829511 {ECO:0000313|EnsemblPlants:KQJ95795};
GN ORFNames=BRADI_3g19046v3 {ECO:0000313|EMBL:KQJ95795.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ95795.1};
RN [1] {ECO:0000313|EMBL:KQJ95795.1, ECO:0000313|EnsemblPlants:KQJ95795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ95795.1,
RC ECO:0000313|EnsemblPlants:KQJ95795};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ95795.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ95795.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ95795}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ95795};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- FUNCTION: Phosphorylates the second messenger diacylglycerol (DAG) to
CC generate phosphatidic acid (PA), another important signaling molecule.
CC PA is required for plant development and responses to abiotic stress
CC and pathogen attack. {ECO:0000256|PIRNR:PIRNR030829}.
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|PIRNR:PIRNR030829,
CC ECO:0000256|RuleBase:RU361128};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|PIRNR:PIRNR030829}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|PIRNR:PIRNR030829,
CC ECO:0000256|RuleBase:RU361128}.
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DR EMBL; CM000882; KQJ95795.1; -; Genomic_DNA.
DR RefSeq; XP_010234517.1; XM_010236215.2.
DR AlphaFoldDB; A0A0Q3I5D8; -.
DR STRING; 15368.A0A0Q3I5D8; -.
DR EnsemblPlants; KQJ95795; KQJ95795; BRADI_3g19046v3.
DR GeneID; 100829511; -.
DR Gramene; KQJ95795; KQJ95795; BRADI_3g19046v3.
DR KEGG; bdi:100829511; -.
DR InParanoid; A0A0Q3I5D8; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
DR ExpressionAtlas; A0A0Q3I5D8; baseline.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR Gene3D; 2.60.200.40; -; 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; IPR016961; Diacylglycerol_kinase_pln.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF102; DIACYLGLYCEROL KINASE; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR PIRSF; PIRSF030829; Diacylglycerol_kinase_pln; 1.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR030829};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR030829};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR030829};
KW Plant defense {ECO:0000256|ARBA:ARBA00022821,
KW ECO:0000256|PIRNR:PIRNR030829};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Stress response {ECO:0000256|PIRNR:PIRNR030829};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR030829}.
FT DOMAIN 123..280
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 57924 MW; ABB5C73A249153DC CRC64;
MRSRSRSCSE MSLSLSAAGS SPAERDGELR SSPNSPPAAA PPPLVGAFIE SLSFRSCGFG
RAASSAFEKE DLRLRAALPQ RLRDALHAAL RARDPSAGKF ALEEAPGAPT GVNQWYALAP
EDAPENPLVA FVNPKSGGRV GPVLKSRLQE LIGEDQVFDL TVVKPSDFVE YALACLEQLA
DSGDHSAKSI RHNLRVMVAG GDGTVGWVLG CLGELYVQNR EPVPPVAVIP LGTGNDLSRS
FGWGASFPFS WKAAAKRSLY KAILGTISCL DSWHIVVSMP EEGEEEEELD LPHSLRHLGE
CTFYDDGTAE GEAPETVSCF AGVFYNYFSI GMDAQVAYGF HQLRDDKPFL ASGPLSNKLI
YAGYTCKQGW FFTQCISDPE LRGLTNIIRL SIKKMDSSEW EHIPVPSSVR AIVALNLHNY
ASGRNPWGNL KPEYLEKKGF VEAQSDDGLL EIFGLKQGWH ASLVMVELIS AKHIAQAAAI
RIEIKGGQWR DAYMQMDGEP WKQPLSTEYS TFVDIKRVPY PSLIINGTDR
//
