ID A0A087GIA6_ARAAL Unreviewed; 486 AA.
AC A0A087GIA6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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 OrderedLocusNames=AALP_Aa7g156200 {ECO:0000313|EMBL:KFK29608.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK29608.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
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; CM002875; KFK29608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087GIA6; -.
DR EnsemblPlants; KFK29608; KFK29608; AALP_AA7G156200.
DR Gramene; KFK29608; KFK29608; AALP_AA7G156200.
DR eggNOG; KOG1169; Eukaryota.
DR OMA; WSIVVSM; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000029120; Chromosome 7.
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:0048366; P:leaf development; IEA:EnsemblPlants.
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 GO; GO:0048364; P:root development; IEA:EnsemblPlants.
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:SF80; DIACYLGLYCEROL KINASE 7; 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:UP000029120};
KW Stress response {ECO:0000256|PIRNR:PIRNR030829};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR030829}.
FT DOMAIN 85..243
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 54123 MW; 3BEF351C76D81328 CRC64;
MEETPRSVGE ASTTEFVKPS ETTSDAVKMR GCGGLGNISW VGVDREELRK RIAMPEYLRL
AMRDCIKRKD VTEIPHHLLL PGDMAPHAPM VVFINPKSGG RHGPVLKQRL QQLMTEEQVF
DLTEVTPHDF VRYGLACLEA VAEKGDECAR ECRERIRIMV AGGDGTVGWV LGCLGELHKD
GKTHIPPVGV IPLGTGNDLS RSFSWGGSFP FAWRSAMKKT LHRATMGSVS RLDSWKIVVS
MPSGEVVDPP HSLKPTEETA LDQALDAEGD VPLKAKSYEG VFYNYFSIGM DAQVAYGFHH
LRNEKPYLAR GPVSNKIIYS SYSCTQGWFC TPCVSNPGLR GLRNIMKIHI KKASCADWEE
IPIPKSVRSI VALNLHNYGS GRHPWGNLKP NYLEKKGFVE AHCDDGLIEI FGLKQGWHAS
FVMAELISAK HIAQAAAVRF ELRGGDWRDA FLQMDGEPWK QPMKTDYSTF VEIKKVPFQS
LMINGE
//
