ID A0A0J7KTV7_LASNI Unreviewed; 1372 AA.
AC A0A0J7KTV7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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};
DE Flags: Fragment;
GN ORFNames=RF55_5988 {ECO:0000313|EMBL:KMQ93882.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ93882.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ93882.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ93882.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic
CC acid (PA). {ECO:0000256|ARBA:ARBA00002064}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, 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:KMQ93882.1}.
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DR EMBL; LBMM01003159; KMQ93882.1; -; Genomic_DNA.
DR STRING; 67767.A0A0J7KTV7; -.
DR PaxDb; 67767-A0A0J7KTV7; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0046486; P:glycerolipid metabolic process; IEA:UniProt.
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 CDD; cd20800; C1_DGK_typeII_rpt1; 1.
DR CDD; cd20852; C1_DGK_typeII_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
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; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF34; DIACYLGLYCEROL KINASE ETA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 2.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
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 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:UP000036403};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..30
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 41..72
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 95..146
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 176..313
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT DOMAIN 1310..1372
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 483..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KMQ93882.1"
SQ SEQUENCE 1372 AA; 151467 MW; 3A4179CC3F1A051D CRC64;
VITPLRSLVL CGENRQDMEE WLNTLRTAAE NRPQGDSGTA ELLGGVTSHG LSCEVCKYKI
HKRCSAKAIN NCKWTTLASI GKDIIEDQDG NITMPHQWME GNLPVSSKCF ICDKTCGSVL
RLQDWRCLWC RATVHTACRP AISIKCPLGP AKLSVVPPTA LHSIGSDEAW EAVRPTGCSP
LLVFVNSKSG DNQGVKFLRR FKQLLNPAQV FDLIKGGPGP GLRLFRHFDP FRILVCSGDG
SVGWVLSEID RLGMHKQCQV GVLPLGTGND LARVLGWGAS CDDDTHLPQL LEKYEKAGTK
MLDRWSIMTF ERSISLPCHK VTLHQPDPAI KSSIAHQYED SVLAHITNIL QSDQESVVIS
SAKVLCETVK DFATHILEVS LNTGDQQLGE KCETLQQKLD LLLQTLSKEE NYLFDNTEEA
DIGTLNSESL SSNQEKGALE KPEKEITNLK KVRRRKSYME RDAVMSRANS LKRAIRRLVE
HTELAVDEQN DPSDEKQGNK MPNITITSDN SPMNSETNIK QHLDISGLLQ TDQTSDNISL
MPTLESGSSL ELSPCPSPTP NVASLSPMPD LRRDSQPEEL LTLPAPDGFA DSRRNSENMP
QGVFSFDSPA AQTAGCQQEA QTTATSDNFL LSSERTQLEA VSDIAVTVTK TTLDTSTPSD
DATMQDTIVS PDTDSLHSRN ISPEHAQKPA KVKLEPRGHV DSDIFDSTKR SESSEIGHID
SPDNSDMLST ETQHSESGLE DLSSLGQDVI SAIMGEKYDS VREGLEIEEP RKSCGLAQFN
EGNDIARQSF KTRNIKMDKE QGMLNKYKTD GLTTCVRVLG TKSMQPVETN IVPVNVEKEK
VSDLLSPVCC FTVSSDNTQA NEKCSINFPP QISVIIDPPS PSLSIESHHK LNLDYNLDPH
DKQYSSGGSM ERLSVELPES GFSPQATRRI SSGSLLKASE VVSLAATTAR LGGSSMSLRH
ERAKSVDKTE DVKKLPIINP LVRLPMWPNV SGGAGLISQA LLANADALCA AVSPLMDPDE
SLMEGYFERC VMNNYFGIGI DAKISLDFHN KREEHPEKCR SRAKNYMWYG VLGSKQWLQK
TYKNLEQRVQ LECDGQRIPL PSLQGIVVLN IPSFMGGTNF WGGSKEGDLF LAPSFDDRIL
EVVAVFGSVQ MAASRLINLQ HHRIAQCQTV QINILGEEGV PIQVDEPELY QVALRTANAL
EQVHPDGKIL QGMSLRPMVT ELVSGARQLY EESCELLRDK GHNLRLREDL ESKLSISLAS
MEQELRKCIF DEGGTGLVYL QNVPADDQFR RFAGNSGAAG HPARDQVTTW GVQEVCTWLE
NLQLGEYADR FVSHDIRGRE LLTLARRDLK ELGITKVGHV KRILQAINDL NN
//
