ID A0A0E0QF41_ORYRU Unreviewed; 502 AA.
AC A0A0E0QF41;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI08G05300.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI08G05300.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) 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 AlphaFoldDB; A0A0E0QF41; -.
DR STRING; 4529.A0A0E0QF41; -.
DR EnsemblPlants; ORUFI08G05300.1; ORUFI08G05300.1; ORUFI08G05300.
DR Gramene; ORUFI08G05300.1; ORUFI08G05300.1; ORUFI08G05300.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_002706_46_2_1; -.
DR OMA; IEKHDYW; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
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:SF47; 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:UP000008022};
KW Stress response {ECO:0000256|PIRNR:PIRNR030829};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR030829}.
FT DOMAIN 41..194
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 443..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 55849 MW; D0B03E893D730864 CRC64;
MEGEMDTVVG SSSKPCGPLT DYHIPDYILR PDAQRVLLDH APPCPVLVFI NSGSGGQLGS
SLIKTYRELL GEAQVFDVSE EAPDKVLHRL NVNLEKLKME GDILAVQIWR TLRIIVAGGD
GTASWLLGVV SDLKLSHPPP IATVPLGTGN NLPFSFGWGK KNPCTDQESV KSFLGLVRHA
KEMKIDSWHI MLRMRATKEG PCDPIAPLEL PHSLHAFHRV SSSDSLNMEG YHTFRGGFWN
YFSMGMDAEI SYGFHSERKK NPEKFKNQLT NQGTYAKVGL KQGWFCASLS HPSSRNIAQL
ASVKIMKRAG SHWQELNIHH SIRSIVCLNL PSFSGGLNPW GTPGTRKVEE RELTAPFVDD
RLIEVVGFRD AWHGLVLLAP NGHGTRLAQA QRIRFEFHKG AAEHTFMRID GEPWKQPLPK
DDDTVVVEIS HLGQVTMLAN EPCKSKSVHD DQSSHAQHSG HGNNDDDKDS MEDEDEWEDG
RRKFGAADTF KIPDEVDIAH LS
//
