ID A8QM13_MAIZE Unreviewed; 495 AA.
AC A8QM13;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
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};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ABO16345.1};
RN [1] {ECO:0000313|EMBL:ABO16345.1}
RP NUCLEOTIDE SEQUENCE.
RA Sui Z.H., Niu L.Y., Zhang J.R.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABO16345.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18824223; DOI=10.1016/j.gene.2008.09.004;
RA Sui Z., Niu L., Yue G., Yang A., Zhang J.;
RT "Cloning and expression analysis of some genes involved in the
RT phosphoinositide and phospholipid signaling pathways from maize (Zea mays
RT L.).";
RL Gene 426:47-56(2008).
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; EF088692; ABO16345.1; -; mRNA.
DR AlphaFoldDB; A8QM13; -.
DR ExpressionAtlas; A8QM13; baseline and differential.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
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; IPR016064; NAD/diacylglycerol_kinase_sf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF98; DIACYLGLYCEROL KINASE 5; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128}.
FT DOMAIN 41..194
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 437..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 55248 MW; ACA28FB3CB87E9D4 CRC64;
MELHRNSTNG SCLSACGPLT DYYIPDYILK PAYEPVTVDN VPCCPVVVFI NSRSGGQLGS
SLIKTYRELL NEAQVFDLSE ESPDKVLHRL YSNFERLKSS GDHVATQIQK SLRLIVAGGD
GTASWLLGVV SDLKLSHPPP VATVPLGTGN NLPFSFGWGK KNPATDQAAV KSFLGQVKGA
REMNIDSWHI IMRMRIPQEG PCDPIAPLDL PHSLHAFHRV SVCDSLNLEG YHTFRGGFWN
YFSLGMDAQV SYEFHSERKR NPEKFRHQLR NQVHTLKLGF KHSLNHLSSR NISQLAKVKI
MKRPGSQWEE LKIPRSIQSV ICLNLPSFSG GLNPWGTPGT RKAQDRDLTA PYVDDGLIEV
VGFRDAWHGL ILLAPNGHGT RLAQAHRIRF EFHKGAAEHT FMRIDGEPWK QPLPKEDDTV
VVEISNLRQV AMLANDPCRS KSVNEPSSPS CHGHEDDDSN SLEDEDEDEW EDGRKKFGAA
ATFKIPDEVD IAHLS
//
