DGKH_DROGR
ID DGKH_DROGR Reviewed; 1941 AA.
AC B4JHJ7;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Diacylglycerol kinase eta {ECO:0000250|UniProtKB:Q86XP1};
DE Short=DAG kinase eta {ECO:0000250|UniProtKB:Q86XP1};
DE EC=2.7.1.107;
GN ORFNames=GH18973;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDV92824.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV92824.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic
CC acid (PA). {ECO:0000250|UniProtKB:Q86XP1}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86XP1}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000255}.
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DR EMBL; CH916369; EDV92824.1; -; Genomic_DNA.
DR RefSeq; XP_001989762.1; XM_001989726.1.
DR AlphaFoldDB; B4JHJ7; -.
DR SMR; B4JHJ7; -.
DR STRING; 7222.FBpp0152879; -.
DR PRIDE; B4JHJ7; -.
DR eggNOG; KOG1170; Eukaryota.
DR HOGENOM; CLU_001799_1_1_1; -.
DR InParanoid; B4JHJ7; -.
DR OMA; FERAHTR; -.
DR PhylomeDB; B4JHJ7; -.
DR Proteomes; UP000001070; 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:diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
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; cd00029; C1; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR11255; PTHR11255; 2.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF111331; SSF111331; 2.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1941
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000375986"
FT DOMAIN 93..186
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 361..497
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT DOMAIN 1878..1941
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 206..256
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 279..330
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1030..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1941 AA; 216882 MW; 3BA4E29CAD1430F9 CRC64;
MSNFLKPNTL HVDSLSPRHR SLSSGLSSGL SSACSSGSVS PVPIIPIIAI SRIRDGDESE
SESEIELEPA RIFHRRMSIN NSGNNKRSTN LASIIKEGYL LKHTWSFQRW RRRYFRLKRN
HLYYAKDAKC DVFDEIDLSE LCYFECSIKN VNHSFQIITP TRSVVLCADS RRDMEDWLGS
LKAATAPQRP RGDSILIDQH DILSNHHHWY ATSHARPTYC NVCRDALSGV TSHGLSCEVC
KCKVHKRCAA KAIANCKWTT LATVGKDIIE QPDGSIIMPH QWMEGNLPVS SICAVCKKTC
GSVLRLQDWR CLWCRDTVHV ACRPQMAIAC PIGPAKLSVV PPTSVHSIST DDAWDVASPK
GNFSPLLVFV NSKSGDNQGV KFLRRFKQLL NPAQVFDLIS TGPSLGLRLF RHFEMFRILV
CSGDGSVGWV LSEIDRFNMH KQCQVAVMPL GTGNDLARVL GWGSSCDDDT HLPQILERYE
SASTKMLDRW SIMVFEKAIS VPKIPKMSIT TEQEAVLTGM VTAANQHLRL IVETNDTQTL
ISSTRNLCDT IDDLVSRIFE HHKDDEQLAV KCDILKQKLT MLLDALQEEE IGAHSGDDLI
ATIRSLIARS VPSTNSARPS LLNPNISIEK TEKDHINLKE RRSSRSLRSS EKEALQCRAN
SVKRAIYNVV EHSEPGRPKR YQRKLSITPF EALKIPTNSG ESTPCSSPLP IIPPINIISP
TMETSRLTCI SPLPDTRRDS VDENFFNSIN LPAPRQFADS RRSSGVPEVI QELEEGANGE
TIYRIGRLSL SGGANIDDAG NRLSPVSDGG DNSPIDRKLD FLRVPIITSD SIVDPLSDYR
PIEVFERTYY MARELDKDKD KERKQDVVLD GEKEEDAGVN EKCEEQTLHP QNTLVHTCNL
QVPGIVVTPQ SQNVYTSDSI TIIDTDQQSN TLQEQSSSEE LGCDASDVLS AISNEECSVA
SEIFDKAETG HTLGDIIQNL DASNFTHIDS PETSDETEAM PGESLMDDIS SVLGHDITNA
LQDNTITDDT TTLCSEHMGP PKPPRKKSMS ALSKSQIHPR RRNSSPPRMA RLARMDSDDN
PQQFGFENIV FEIDNRCDDQ KMREPPRYCS LAQFVEGNDI ARQSFKQLML ECNSNNNSNN
NSNSNSNNNN HNDGNSNDEP ETPTNTVITL AHSQLTTTST SDELDELSTQ TAIKIEIHDA
DSSTMCTTTA TTKPLESAMA SSTSPTKRSG LGQDISVVVR PPTPLRGDSI KPTPSSSSIL
SSSLLGVRSL NSSEIRRHSS HAPSLAVREY DKDKDRRHSG FNPNYLALDP EHARFLSSSP
AASRRISCGS LFKKNQKYYT KRTYGLFRVR FFVVAEPDIR LATLALIRPL IPLPNEALPN
LQTLKGSKSS LFMGSTLFGF EHFSDKEERQ GKDKERTPPE ETSRKMPIIN PIVRLPNWPN
LANGTGFISK CLLANADTLC AAVSPLMDPD ETLLAGYHEK CVMNNYFGIG IDAKISLDFH
NKREEHPEKC RSRARNYMWY GVLGSKQLLQ KTCKNLEQRV QLECDGQRIP LPELQGIVIL
NIPSFMGGTN FWGSSTKKDD IFLPPSFDDR VLEVVAVFGS VQMAASRLIN LQHHRIAQCQ
SVQINILGDE EIPIQVDGEA WLQPPGMIRI LHKNRVQMLC RNRSLEVSLK SWQEKQRQHS
ISIQRDASST ASEHAVSTDD VISERECYVL LNFIEAVSSL VKWVKFLIIS HPALQHDLYE
VACRASEALE SIHPQGKLLE GPSLRTKLVE VIDSSRQLYD DACTLLRDRG HSLILREDLE
TKLSAALANM EMELKKCSVQ KCIDGKLRAY FNVLAPNEES DGRRKSRPFW VRLRSGSTAG
QQQFKPPMTN TREAANNWSV NEVVTWLETM QLSEYVDSFL KNDIRGKELL TLGRRDLKDL
GVVKVGHVKR ILQAIKDLSE N
