ID G0N7N7_CAEBE Unreviewed; 940 AA.
AC G0N7N7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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};
GN Name=Cbn-dgk-1 {ECO:0000313|EMBL:EGT54820.1};
GN ORFNames=CAEBREN_23338 {ECO:0000313|EMBL:EGT54820.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001383,
CC ECO:0000256|RuleBase:RU361128};
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR EMBL; GL379848; EGT54820.1; -; Genomic_DNA.
DR AlphaFoldDB; G0N7N7; -.
DR STRING; 135651.G0N7N7; -.
DR EnsemblMetazoa; CBN23338.1; CBN23338.1; WBGene00162063.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_003770_0_0_1; -.
DR InParanoid; G0N7N7; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IEA:EnsemblMetazoa.
DR GO; GO:0044297; C:cell body; IEA:EnsemblMetazoa.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:EnsemblMetazoa.
DR GO; GO:0045202; C:synapse; IEA:GOC.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:EnsemblMetazoa.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0046834; P:lipid phosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0040013; P:negative regulation of locomotion; IEA:EnsemblMetazoa.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:2000292; P:regulation of defecation; IEA:EnsemblMetazoa.
DR GO; GO:0046662; P:regulation of egg-laying behavior; IEA:EnsemblMetazoa.
DR GO; GO:0032094; P:response to food; IEA:EnsemblMetazoa.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IEA:EnsemblMetazoa.
DR CDD; cd20803; C1_DGKtheta_typeV_rpt1; 1.
DR CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1.
DR CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1.
DR CDD; cd17111; RA1_DAGK-theta; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
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 InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001965; Znf_PHD.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00788; RA; 2.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00314; RA; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 3.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50200; RA; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 20..70
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 83..131
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 149..200
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 264..353
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 355..454
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 534..672
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 882..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 105432 MW; AA7CC7935E8A5101 CRC64;
MAAEGHNVDA NLVDMRPNHG HYFVKKTFGK PTYCHHCCDK IWGMLTTGYS CEMCNFICHE
KCLRTVVSYC SSVALQLIKN PVAHTWSAPC LIKRKYCCVC RKRTDEAMSV ECEVCEYYVH
VDCSDLAVSD CKEAATYVAN MESANAVQYH HMREGNLPKE SKCVVCRKTC FSTECLAGMR
CEWCGQTAHA VCYRQMDKEC DFGVLRKIVL PPMCLTIPRT ELPMEQLLNI SSHDQPQSRK
VSSPSKIQAD DVSTTAEEIK ERDDFEVIRV FDGNNSYRLQ ISRNIIVAKH VSVQQVRDAA
LRRFHINDTP ERYYITQVVG EVEEEILEDP VPLRNVKRPE GKRAQIFIRY YDDPDKDEVK
VYGGWLRKVP VTFCAISVSK DTIVQDLVTD ALYHFGLDGA LWNRYNLIEV SLDRGVAERT
CNPQENVLQL VRNLRKDSLR RYHVVRFYVQ EKEDPHDHAV FVGNLPVSLA QRQYERILLK
LLGAKEKPFT AIGPIYFEYG SLIITFNTPK AATAAEKKLI VLCLPNVQPQ MIPKDVEPLL
VLVNVKSGGC QGTELIQSFR KLLNPFQVFD VLNGGPLVGL YVFRNIPKYK ILACGGDGTI
GWVLQCLDIA KQDAACFSPP CGIVPLGTGN DLARVLRWGG GYTGEENPMD ILKDVIEADT
VKLDRWAVVF HEEERNQPTS SGTQTEMSEQ TMNNPEDQTS MIIMNNYFGI GIDADVCLKF
HNKRDANPEK FQSRLFNKTQ YAKIGLQKMF FERTCKDLFK RIELEVDGRT IELPNIEGIV
VLNLLSWGSG ANPWGTSKEE GNFSKPTHYD GLLEVVGISD VSRLGLIQSK LAAGIRIAQG
GSIRITTHEE WPVQVDGEPH IQPPGTITIL KSALKAQMLK KAKKSRRGGN ASSLLNQAQD
TTDPLSGPLG VPSTLGDPQH GKTTPDNTAA DSDEEGDAFL
//
