DGKH_DROER
ID DGKH_DROER Reviewed; 1918 AA.
AC B3NYS4;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 73.
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=GG14241;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV48187.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV48187.1};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDV48187.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH954181; EDV48187.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001979229.2; XM_001979193.2.
DR AlphaFoldDB; B3NYS4; -.
DR SMR; B3NYS4; -.
DR STRING; 7220.FBpp0132787; -.
DR PRIDE; B3NYS4; -.
DR eggNOG; KOG1170; Eukaryota.
DR Proteomes; UP000008711; 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; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1918
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000375985"
FT DOMAIN 82..175
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 350..486
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT DOMAIN 1855..1918
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 195..245
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 268..319
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1918 AA; 214106 MW; F15B3649942C3926 CRC64;
MAHLKLDTLH VQRSPRGSRR SSPSSGRSSA CSSGSISPVP IIPIISISHD GDESESESEI
ETEPVRLFQR RMSTKCTNNL AAIIKEGFLL KHTWSFQRWR RRYFRLKRNM LFYAKDEKCD
VFDDIDLSDL CYFECGIKNV NHSFQIITPT RSLVLCAESR REMEDWLGGL KTATAPQRPR
GDSFLIEQHD ILSNHHHWYA TSHARPTYCN VCRDALSGVT SHGLSCEVCK CKVHKRCAAK
SIANCKWTTL ASVGKDIIEQ ADGSIIMPHQ WMEGNLPVSS MCAVCKKTCG SVLRLQDWRC
LWCRATVHVA CRPQMAVACP IGPAKLSVVP PTSVHSISTD DAWDVASPKG NFSPLLVFVN
SKSGDNQGVK FLRRFKQLLN PAQVFDLIST GPSLGLRLFR HFEMFRILVC SGDGSVGWVL
SEIDRFNMHK QCQVAVMPLG TGNDLARVLG WGSSCDDDTH LPQILERYES ASTKMLDRWS
IMVFEKAIPV PKTPKMSIST EQEAMLTGMV TSANHHLRFI VETNDTQTLI SSTRNLCDTV
DDLVCRISEH HKEDEQLAVK CDILRQKLNM LLDALQEEEI GAHSGDDLIA TIRSLITRSI
PVTPGSNAYL LNPNISIEKT EKDQINTKER RNSRSLRSSE KEALQCRANS VKRAIYNVVE
HSEPGRPKRY QRKLSITPFE ALKLPTTASG ESTPCTSPLP IIPPINIISP TMETSRLTCI
SPLPDTRRDS VDENFFNSIN LPAPRQFADS RRSSGVPEVI QEIEEGANGE TVYRRSRMSL
TGGANIDDAG NRLSPCSDGG ENTPTERKVD FLRVPIHTGE PIVDPLCDYR PHEVFERTYY
MTREMDKDKE KDKEKEKEKT AEIEEENDKC VEKLGSIPAE KLVHTCNLQV PGVVVTPNPQ
NVYSSASITI IDTDAQTTTE QSSSDDLGGE ASDVLSAISN EECSVASEIF DKQDAGQTVG
DIIQNMDASN FTHIDSPETS DETEAMPGES LMDDISSVLG HDITYALQDN TLTDDTTTLC
SEHAGPPKPP RKKSLSALSR TQAHPRRRNS SPPRTARLAR MDSDDNPQQF GFENIVFEID
NRCDDQKMRE PPRYCSLAQF VEGNDIARQS FKQLMLEQHR GGDNDIESPE QQQAPTNKGA
HLLATTSEDE LSTQTAIKIE IHDIDATVRS INSSMKPNTI LTTSTSPTKK SGHGQDISVV
VRPPTPLRGD SIKPTVSLLP VSSGGAMAVS MTCSGMLGVR AMNASEIRRH SSHAPSLAVR
EFDKDKDRRH SGFNPNQLTL DPEHARFLSS SPAASRRISC GSLFKKKNKK IATKRSYGLF
SVRFFVVAEP DFRLATLALI RPLIPLPNEA LPNLQTLKGS KSSLFMGSTL FGFDHLASAE
RDKEERGGKD KDKTPTEEAN RKLPIINPLV RLPNWPNLAN GGGFISKCLL ANADTLCAAV
SPLMDPDETL LAGYHEKCVM NNYFGIGIDA KISLDFHNKR EEHPEKCRSR ARNYMWYGVL
GSKQLLQKTC KNLEQRVQLE CDGQRIPLPE LQGIVILNIP SFMGGTNFWG SSTKKDDIFL
PPSFDDRVLE VVAVFGSVQM AASRLINLQH HRIAQCQSVQ INILGDEEIP IQVDGEAWLQ
PPGMIRILHK NRVQMLCRNR SLELSLKSWH EKQRQHSISI QRDASSTASE HANSTDEVIS
ERECYVLLNF IEAVSSLVKW VKFLIISHPA LQHDLYEVAC RASEALESIH PQGKLLEGPS
LRTKLVEVID SSRQLYDDAC TLLRDRGHSL ILREDLETKL SAALANMEME LKKCSVQKCI
DGKLRAYFNV LAPNEESDGR RKSRPFWVRL RSGSTAGQQV FKPPLTNTRE AANNWSVNEV
VTWLETMQLS EYVDSFLKND IRGKELLTLG RRDLKDLGVV KVGHVKRILQ AIKDLSEN
