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Database: UniProt
Entry: A0A2T7D5B4_9POAL
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ID   A0A2T7D5B4_9POAL        Unreviewed;       516 AA.
AC   A0A2T7D5B4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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   ORFNames=GQ55_6G088200 {ECO:0000313|EMBL:PUZ50791.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ50791.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ50791.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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; CM009754; PUZ50791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7D5B4; -.
DR   STRING; 1504633.A0A2T7D5B4; -.
DR   EnsemblPlants; PUZ50791; PUZ50791; GQ55_6G088200.
DR   Gramene; PUZ50791; PUZ50791; GQ55_6G088200.
DR   Proteomes; UP000244336; Chromosome 6.
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:UP000244336};
KW   Stress response {ECO:0000256|PIRNR:PIRNR030829};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR030829}.
FT   DOMAIN          108..267
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..30
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  56471 MW;  215F40D9158440B0 CRC64;
     MSSFSSSAPS PTPSEREAPR SPPPPAPPLV GALIESLSFR SCGFGRAAAS AFEKEDLRAR
     AAFPRRLRAA VHAAMRARDP AAGSFALEDR DGDGSCHPWF DAAAHDSAPE SPLVAFVNPR
     SGGRLGPVLK TRLQELIGED QVFDLTIVKP SDFVEYALAC LEQLAESGDH SARFVRDNLR
     VMVAGGDGTV GWVLGCLGEL YVQNRGPVPP VAVIPLGTGN DLSRSFGWGA SFSFSWKASA
     KRSLYKAIFG SVSCLDSWHV VVSVPENGEE EKEELDLPHS LRRLGQCTFY DDGTAKGELP
     ETVSCFDGVF YNYFSIGMDA QVAYGFHQLR DEKPFLASGP LSNKLIYAGY TCKQGWFFTQ
     CISDPELRGL RNIICLSIKR MDSSEWESIS VPSSVRAIVA LNLHNYASGR NPWGNLKPEY
     LEKRGFVEAH SDDGLLEIFG LKQGWHASLV MVELISAKHI AQAAAIRIEI KGGQWRDAFM
     QMDGEPWKQP LSSEYSTFVD IKKVPYPSLI INGGDR
//
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