ID E3LSL8_CAERE Unreviewed; 794 AA.
AC E3LSL8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=Cre-dgk-3 {ECO:0000313|EMBL:EFP09339.1};
GN ORFNames=CRE_25613 {ECO:0000313|EMBL:EFP09339.1}, FL81_13374
GN {ECO:0000313|EMBL:POM40656.1}, FL82_20456
GN {ECO:0000313|EMBL:OZF75302.1}, GCK72_009370
GN {ECO:0000313|EMBL:KAF1761116.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFP09339.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|EMBL:EFP09339.1};
RG The Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:POM40656.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM40656.1};
RX PubMed=26114425; DOI=10.1371/journal.pgen.1005323;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Reproductive Mode and the Evolution of Genome Size and Structure in
RT Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005323-e1005323(2015).
RN [4] {ECO:0000313|EMBL:POM40656.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM40656.1};
RX PubMed=26394399; DOI=10.1371/journal.pgen.1005497;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Correction: Reproductive Mode and the Evolution of Genome Size and
RT Structure in Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005497-e1005497(2015).
RN [5] {ECO:0000313|EMBL:OZF75302.1, ECO:0000313|Proteomes:UP000216624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX439 {ECO:0000313|EMBL:OZF75302.1,
RC ECO:0000313|Proteomes:UP000216624};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:POM40656.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PX356 {ECO:0000313|EMBL:POM40656.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:KAF1761116.1, ECO:0000313|Proteomes:UP000483820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX506 {ECO:0000313|EMBL:KAF1761116.1,
RC ECO:0000313|Proteomes:UP000483820};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KAF1761116.1};
RA Teterina A.A., Willis J.H., Phillips P.C.;
RT "Chromosome-level assembly of the Caenorhabditis remanei genome.";
RL Submitted (DEC-2019) 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; DS268414; EFP09339.1; -; Genomic_DNA.
DR EMBL; WUAV01000003; KAF1761116.1; -; Genomic_DNA.
DR EMBL; NMWX01000910; OZF75302.1; -; Genomic_DNA.
DR EMBL; LFJK02000063; POM40656.1; -; Genomic_DNA.
DR RefSeq; XP_003113085.1; XM_003113037.1.
DR AlphaFoldDB; E3LSL8; -.
DR STRING; 31234.E3LSL8; -.
DR EnsemblMetazoa; CRE25613.1; CRE25613.1; WBGene00055153.
DR GeneID; 9818528; -.
DR KEGG; crq:GCK72_009370; -.
DR CTD; 9818528; -.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_003770_1_0_1; -.
DR OMA; QTHKSFP; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR Proteomes; UP000216624; Unassembled WGS sequence.
DR Proteomes; UP000483820; Chromosome iii.
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:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042048; P:olfactory behavior; IEA:EnsemblMetazoa.
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 GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:EnsemblMetazoa.
DR GO; GO:0043052; P:thermotaxis; IEA:EnsemblMetazoa.
DR CDD; cd20851; C1_DGK_typeI_like_rpt2; 1.
DR CDD; cd20799; C1_DGK_typeI_rpt1; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF48; DIACYLGLYCEROL KINASE 1; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF14513; DAG_kinase_N; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
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:UP000008281};
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 170..205
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 215..250
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 265..316
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 329..375
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 423..558
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 794 AA; 89221 MW; 70AA178A4BF40FE6 CRC64;
MLLSPEQFSR LSEYAAYSRR KLKDMLSDFQ QDGKFYSYLS VDGQTINIDG FRAFLIDYFG
ADLPSDLVDQ LFLSFSKPPI KERRTSLFED AISTVRAKFT DTLSGRMTGL NIAGGSGQQT
DRSTGSEPQA LVCIPEDDVM GPKAATNESQ EPRIPLKPLI CTLSLLEADT PENKLDVVFH
VYDSDGNGFL DKSEIDGIIE QMMNVARYQQ WDTIELEQII RQMMVDIDYD NDGIVSFDEW
RRGGLTNIPL LVLLGFDTEM KEDGSHVWRL RHFTKPTYCN ACCSILVGWG GKQGLSCSLC
KYTVHERCVR SAATNCIRTY SSRQQDKLYH HWQDANATAK CVKCKATVGV FQGKGCRWCH
NYVHHRCMSA LAQECDLGAL VHHILPPTHI FPAFLERKTS TSLKNHNFGS HSASLLQAIS
PSNDCRPLLV LVNPKSGGKQ GVKILQKFEY LLNPRQVYDL SKTGPEPGLQ LFSTLKNCNI
LVCGGDGTIG WVLESMDKMT FPHGRPPVAV LPLGTGNDLA RCLRWGGGYE NENLHKILEQ
IEKSSLIDMD RWQIKIEITE NKNTRRASEK GDSPPYSIIN NYFSIGVDAS IAHRFHVMRE
KFPEKFNSRM RNKLWYFELG TSETLSSSCK NLHEQIDILC DGESIDLGQD ASLEGIALLN
IPSIYGGSNL WGRSRKSKSR MGLFPMKNAE KMQLQTRVQD IGDGLIELVG LESAMQMGQI
KAGVRGARRL SQCSTVVIQT HKSFPMQIDG EPWMQPPCII QITHKNQAKM LVAAAPRKRS
SWMLLKRQST NDDN
//