DGKH_DROSE
ID DGKH_DROSE Reviewed; 1914 AA.
AC B4I4Y1;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 71.
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=GM10981;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW55274.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW55274.1};
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=EDW55274.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH480821; EDW55274.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002038737.1; XM_002038701.1.
DR AlphaFoldDB; B4I4Y1; -.
DR SMR; B4I4Y1; -.
DR STRING; 7238.B4I4Y1; -.
DR Proteomes; UP000001292; 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..1914
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000375989"
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 1851..1914
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 621..642
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 1016..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1216
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 621..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1914 AA; 213869 MW; 8F3D5EECF74C2777 CRC64;
MSHLKLDTLH VQRSPRGSRR SSRSSGRSSA CSSGSISPVP IIPIISISHD GDESESESEI
ETEPARLFQR RMSIKCTNNL AAIIKEGFLL KHTWSFQRWR RRYFRLKRNM 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 VETNDTQTLI SSTRNLCDTV
DDLVCRISEH HKDDEQLAVK CDILRQKLNM LLDALQEEEI GAHSGDDLIA TIRSLIARSI
PVTPGSNAYL LNPNISIEKT EKDQINSKER RNSRSLRSSE KEALQCRANS VKRAIYNVVE
HSEPGRPKRY QRKLSITPFE ALKLPTNASG ESTPCTSPLP IIPPINIISP TMETSRLTCI
SPLPDTRRDS VDENFFNSIN LPAPRQFADS RRSSGVPEVI QEIEEGANGE TVYRRSRMSL
TGGANIDDAG NRLSPCSDGG ENTPTERKLD FLRVPIHTGE PIVDPLCDYR PHEVFERNYY
MTREMDKDKE KDKEKDKPVE IDIEKDTCVE KEGSMPEEKL VHTCNLQVPG VVVTPNPQNV
YSSASITIID TDAQTTTEQS SSDDLGGEAS DVLSAISNEE CSVASEIFDK QDAGQTVGDI
IQNMDASNFT HIDSPETSDE TEAMPGESIM DDISSVLGHD ITYALQDNTL TDDTTTLCSE
HVGPPKPPRK KSLSALSRTQ AHPRRRNSSP PRIARLARMD SDDNPQQFGF ENIVFEIDNR
CDDQKMREPP RYCSLAQFVE GNDIARQSFK QLMLEQHRGG DNDSEYPEHQ QTPTNKGANL
LITTSEDELS TQTAIKIEIQ DIDATVRNLN SSMKPNTILT TSTSPTKKSG HGQDISVVVR
PPTPLRGDST KPTVSLLPVS SGGAMAVSMT CSGMLGVRAM NASEIRRHSS HAPGLAVREF
DKDKDRRHSG FNPNQLTLDP EHARFLSSSP AASRRISCGS LFKKKNKQIA TKRSYGLFSV
RFFVVAEPDF RLATLALIRP LIPLNEALPN LQTLKGSKSS LFMGSTLFGF DHLASAEKDK
EEKGGKDKEK TPTEETNRKL PIINPLVRLP NWPLANGGGF ISKCLLANAD TLCAAVSPLM
DPDETLLAGY HEKCVMNNYF GIGIDAKISL DFHNKREEHP EKCRSRARNY MWYGVLGSKQ
LLQKTCKNLE QRVQLECDGQ RIPLPELQGI VILNIPSFMG GTNFWGSSTK KDDIFLPPSF
DDRVLEVVAV FGSVQMAASR LINLQHHRIA QCQSVQINIL GDEEIPIQVD GEAWLQPPGM
IRILHKNRVQ MLCRNRSLEL SLKSWQEKQR QHSISIQRDA SSTASEHANS TDEVISEREC
YVLLNFIEAV SSLVKWVKFL IISHPALQHD LYEVACRASE ALESIHPQGK LLEGPSLRTK
LVEVIDSSRQ LYDDACTLLR DRGHSLILRE DLETKLSAAL ANMEMELKKC SVQKCIDGKL
RAYFNVLAPN EESDGRRKSR PFWVRLRSGS TAGQQAFKPP LTNTREAPNN WSVNEVVTWL
ETMQLSEYVD SFLKNDIRGK ELLTLGRRDL KDLGVVKVGH VKRILQAIKD LSEN
