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Database: UniProt
Entry: A0A371F681_MUCPR
LinkDB: A0A371F681_MUCPR
Original site: A0A371F681_MUCPR 
ID   A0A371F681_MUCPR        Unreviewed;       485 AA.
AC   A0A371F681;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=DGK5 {ECO:0000313|EMBL:RDX73812.1};
GN   ORFNames=CR513_46521 {ECO:0000313|EMBL:RDX73812.1};
OS   Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX   NCBI_TaxID=157652 {ECO:0000313|EMBL:RDX73812.1, ECO:0000313|Proteomes:UP000257109};
RN   [1] {ECO:0000313|EMBL:RDX73812.1, ECO:0000313|Proteomes:UP000257109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC   TISSUE=Seed {ECO:0000313|EMBL:RDX73812.1};
RA   Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT   "Draft genome of Mucuna pruriens seed.";
RL   Submitted (MAY-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDX73812.1}.
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DR   EMBL; QJKJ01010400; RDX73812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371F681; -.
DR   STRING; 157652.A0A371F681; -.
DR   Proteomes; UP000257109; 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:SF101; 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   Stress response {ECO:0000256|PIRNR:PIRNR030829};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR030829}.
FT   DOMAIN          36..189
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          434..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  54012 MW;  CF1A5BDF7C5B0099 CRC64;
     MASHTSDASF LKNFWIPNHV LVPESVAEGS KVDREGPKCP VLVFVNSRSG GQLGGDLLKT
     YRALLNEKQV FDLGEEAPDK VLSRIYANLE NLKLQGDQIA ITIMEKLRLI VAGGDGTAGW
     LLGVVCDLKL SHPPPIATVP LGTGNNLPFA FGWGKKNPGT DEQSVKSFLD QVMKAEEMKI
     DNWHILMRMR APKQGSCDPI APLELPHSLH AFHRVSEADE LNKEGCHTFR GGFWNYFSMG
     MDAQVSYAFH SERKLHPEKF KNQLVNQSTY AKLGCTQGWF FAPLFHPPSS NIAHLAKVKV
     MKTHGHWEDL HIPSSIRSIV CLNLPSFSGG LNPWGTPNRM KRRDRGLTPP YVDDGLIEVV
     GFRDAWHGLV LLAPNGHGTR LAQARRILFE FHKGAADHTF MRIDGEPWKQ PLPVDDDTVS
     VEISHHGQVN MLATHDSKSK SVNAPYHNDE EDDSDDEDSK ADEFRKFGAA ETFKIPDEVD
     LAHLS
//
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