DGKH_DROAN
ID DGKH_DROAN Reviewed; 1916 AA.
AC B3LXF2;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 76.
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=GF18176;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV42796.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV42796.1};
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=EDV42796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH902617; EDV42796.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001954235.2; XM_001954199.2.
DR AlphaFoldDB; B3LXF2; -.
DR SMR; B3LXF2; -.
DR STRING; 7217.FBpp0121368; -.
DR PRIDE; B3LXF2; -.
DR GeneID; 6500954; -.
DR KEGG; dan:6500954; -.
DR eggNOG; KOG1170; Eukaryota.
DR InParanoid; B3LXF2; -.
DR Proteomes; UP000007801; 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..1916
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000375984"
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 1853..1916
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..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1053
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1916 AA; 213112 MW; E49E3E9A4D283BA2 CRC64;
MAHIKLDTLD VVQRPGTTRR SNSNSGRSSA CSSGSLSPVP IIPIIAISRD TDDSESESEI
ETEPARLFQR RMSIKCTNNL AAIIKEGFLL KHTWSFQRWR RRYFRLKRNV LFHAKDFQCD
VLDEIDLSDL CYFECGIKNV NHSSQIITPT RSLVLCAESR REMEDWLGSL KTATTPQRPR
GDSFLIEQHD ILSNHHHWYA TSHARPTYCN VCRDALSGVT SHGLSCEVCK CKVHKRCAAK
SIANCKWTTL ASVGKDIIEQ ADGSIIMPHQ WMEGNLPVSS VCAVCKKTCG SVLRLQDWRC
LWCRATVHVA CRPQMAVACP IGPAKLSVVP PTSVHSISTD DAWDVASPKG NFSPLLVFVN
SKSGDNQGVK FLRRFKQLLN PAQVFDLIST GPSLGLRLFR HFEMFRILVC SGDGSVGWVL
SEIDRFNMHK QCQVAVMPLG TGNDLARVLG WGSSCDDDTH LPQILERYES ASTKMLDRWS
IMVFEKAIAV PKTPKMSITT EQEALLTGMV TSANHHLRFI VETNDTQTLI SSTQSLCDTI
DDLVGRISEH HREDEQLAVK CDILRQKLNM LLDALQEEEM GAHSGDDLIA TIRSLIARSI
PQTPGTSAPL LNPSISIEKN EKDEINTKER RSSRSLRSSE KEALQSRANS VKRAIYNVVE
HSEPGRPKRY QRKLSITPFE ALKLPTTASG DSTPCSSPLP IIPPINIISP TMETSRLTCI
SPLPDTRRDS VDESFFNSIS LPAPRQFADS RRSSGVPDVI QEIEEGANGE TVYRIGRMSL
SGGANIDDAG NRLSPCSDGG ENTPTERKVD FLRVPILTGE PIVDPLSDYR PIEVFERTYY
MNRELDRGKE GTEEKKGDIE KEKSSGTDVE KEDNMPTEKQ ALVHICNLQV PGIVVTPNSQ
NVYTSASLTI IDTDAQTTNE QSSSEEIAGE ASDVLSAISN EECSVASEIF DKQDAGHTLG
DIIQSLDASN FTHIDSPETS DETEAMPGES IMDDISSVLG HDITYALQDN TLTDDTTTLC
SEHVGPPKPP RKKSLSALTR GHSHPRRRNS SPPRIPRLAR MDSDDNPQQF GFENIVFEID
NRCDDQKMRE PPRYCSLAQF VEGNDIARQS FKQLMLEQHG SNDNDTEYPE QQTPTNTMTN
LMATTSEDEL STQTAIKIEI QDVDATMVRN INSSMKANTI LTTSTSPTKK SGHGQDISVV
VRPPTPLRGD SVKPSGSLLL DGSGGAISMA MGCSSLLGVR AMNAEIRRHS SHAPGLAVRE
IDKDKDRRHS GFNPNLLTLD PEHARFLSSS PAASRRISCG SLFKKNQKIA TKRGYGLFSV
RFLVVAEPDI RLATLALIRP LIPLPNEALP NLQTLKGSKS SLFMGSTLFG FDQFAAGDKE
KDEKGCKDKE KTPTEETGRK LPIINPLVRL PNWPNLANGG GFISKCLLAN ADTLCAAVSP
LMDPDETLLA GYHEKCVMNN YFGIGIDAKI SLDFHNKREE HPEKCRSRAR NYMWYGVLGS
KQLLQKTCKN LEQRVQLECD GQRIPLPELQ GIVILNIPSF MGGTNFWGSS TKKDDIFLPP
SFDDRVLEVV AVFGSVQMAA SRLINLQHHR IAQCQSVQIN ILGDEEIPIQ VDGEAWLQPP
GMIRILHKNR VQMLCRNRSL ELSLKSWQEK QRQHSISIQR DTSSTTSEHA TSTDEVISER
ECYVLLNFIE AVSSLVKWVK FLIISHPALQ HDLYAVACRA SEALESIHPQ GKLLEGPSLR
TKLVEVIDSS RQLYDDACTL LRDRGHSLIL REDLETKLSA ALANMEMELK KCSVQKCIDG
KLRAYFNVLA PNEEPDARRK SRPFWVRLRS GSTAGQQAFK PPLTNTREAA NNWSVNEVVT
WLETMQLSEY VDSFLKNDIR GKELITLGRR DLKDLGVVKV GHVKRILQAI KDLSEN
