ID DGKH_DROYA Reviewed; 1917 AA.
AC B4PRE2;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 27-MAR-2024, entry version 84.
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=GE24946;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW96330.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW96330.1};
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=EDW96330.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000160; EDW96330.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002096618.2; XM_002096582.2.
DR AlphaFoldDB; B4PRE2; -.
DR SMR; B4PRE2; -.
DR GeneID; 6536003; -.
DR eggNOG; KOG1170; Eukaryota.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000002282; Chromosome 3R.
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 CDD; cd13274; PH_DGK_type2; 1.
DR CDD; cd09507; SAM_DGK-delta-eta; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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; IPR011993; PH-like_dom_sf.
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; 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; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
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; 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..1917
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000375991"
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 1854..1917
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 1015..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1149
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 18..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1917 AA; 214006 MW; C373CA1DE34FDBA5 CRC64;
MSHLKLDTLH VQRSPRGSRR SSRSSGRSSA CSSGSISPVP IIPIISISHD GDESESESEI
ETEPARLFQR RMSIKCTNNL AAIIKEGFLL KHTWSFQRWR RRYFPLKRNM LFYAKDEKCD
VFDDIDLSDL CYFECGIKNV NHSFQIITPT RSLVLCAESR REMEDWLGSL 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 VETSDTQTLI SSTRNLCDTV
DDLVCRISEH HKDDEQLAVK CEILRQKLNM LLDALQEEEM GAHSGDDLIA TIRSLIARSI
PVTPGSSAYL LNPNISIEKT EKDQINTKER RNSRSLRSSE KEALQCRANS VKRAIYNVVE
HSEPGRPKRY QRKLSITPFE ALKLPTTASG ESSPCTSPLP IIPPINIISP TMETSRLTCI
SPLPDTRRDS VDENFFNSIN LPAPRQFADS RRSSGVPEVI QEIEEGANGE TMYRRCRMSL
TGGANIDDAG NRLSPCSDGG ENTPTERKVD FLRVPIHTGE PIVDPLCDYR PHEVFERTYY
MTREMDKDKE KDKENDKTVE IDKEKDNCVA KEDSIPAERL VHTCNLQVPG VVVTPNTQNV
YSSASITIID TDAQTTTEQS SSDDLGGEAS DILSAISNEE CSVASEIFDK QDAGQTVGDI
IQNMDASNFT HIDSPETSDE TEAMPGESIM DDISSVLGHD ITYALQDNTL TDDTTTLCSE
HAGPPKPPRK KSLSALSRTQ AHPRRRNSSP PRIARLARMD SDDNPQQFGF ENIVFEIDNR
CDDQKMREPP RYCSLAQFVE GNDIARQSFK QLMLEQQQRD GDNDTEYPEQ QQTPTNKGPN
SLATTSEDEL SAQTAIKIEI HDIDATVRNI NSSMKPNTIL TTSTSPTKKS GHGQDISVVV
RPPTPLRGDS IKPTASLMPV SSGGAMAVSM NCSGMLGVRA MNASEIRRHS SHAPGLAVRE
FDKDKDRRHS GFNPNQLTLD PEHARFLSSS PAASRRISCG SLFKKKNKKI ATKRSYGLFS
VRFFVVAEPD FRLATLALIR PLIPLPNEAL PNLQSLKGSK SSLFMGSTLF GFDHLASAEK
DKDEKGGKDK DKTPTEETNR KLPIINPLVR LPNWPNLANG GGFISKCLLA NADTLCAAVS
PLMDPDETLL AGYHEKCVMN NYFGIGIDAK ISLDFHNKRE EHPEKCRSRA RNYMWYGVLG
SKQLLQKTCK NLEQRVQLEC DGQRIPLPEL QGIVILNIPS FMGGTNFWGS STKKDDIFLP
PSFDDRVLEV VAVFGSVQMA ASRLINLQHH RIAQCQSVQI NILGDEEIPI QVDGEAWLQP
PGMIRILHKN RVQMLCRNRS LELSLKSWQE KQRQHSISIQ RDASSTASEH ANSTDEVISE
RECYVLLNFI EAVSSLVKWV KFLIISHPAL QHDLYEVACR ASEALESIHP QGKLLEGPSL
RTKLVEVIDS SRQLYDDACT LLRDRGHSLI LREDLETKLS AALANMEMEL KKCSVQKCID
GKLRAYFNVL APNEESDGRR KSRPFWVRLR SGSTAGQQAF KPPLTNTREA ASNWSVNEVV
TWLETMQLSE YVDSFLKNDI RGKELLTLGR RDLKDLGVVK VGHVKRILQA IKDLSEN
//
