DGKH_DROMO
ID DGKH_DROMO Reviewed; 1925 AA.
AC B4K6T8;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=GI24133;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW14204.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW14204.1};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH933806; EDW14204.1; -; Genomic_DNA.
DR RefSeq; XP_001998743.2; XM_001998707.2.
DR AlphaFoldDB; B4K6T8; -.
DR SMR; B4K6T8; -.
DR STRING; 7230.FBpp0173350; -.
DR eggNOG; KOG1170; Eukaryota.
DR HOGENOM; CLU_001799_1_1_1; -.
DR InParanoid; B4K6T8; -.
DR OMA; FERAHTR; -.
DR PhylomeDB; B4K6T8; -.
DR Proteomes; UP000009192; 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..1925
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000375988"
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 1862..1925
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 620..641
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 847..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1925 AA; 214943 MW; 6D8E3E275A23BCF2 CRC64;
MANLKPNTLH VDNLSPRQRS LSSGLSSACS SGSVSPVPII PIISISRDGE ESETESEIEP
EPARIFHRRM STHSKRNNNL SAIIREGYLM KHTWSFQRWR RRYFRLKRSY LYYAKDAKCD
VFDEIDLSEL CYFECSIKNV NHSFQIITPT RSLVLCADSR REMEDWLGSL KTATAPQRPR
GDSFLIDQHD ILSNHHHWYA TSHARPTYCN VCRDALSGVT SHGLSCEVCK CKVHKRCAAK
AIANCKWTTL ATVGKDIIEQ PDGSLIMPHQ WMEGNLPVSA VCAVCKKTCG SVLRLQDWRC
LWCRDTVHVA CRPQMPIVCP IGPAKLSVVP PTSVHSISTD DAWDVVSPKG NFSPLLVFVN
SKSGDNQGVK FLRRFKQLLN PAQVFDLIST GPSLGLRLFR HFEMFRILVC SGDGSVGWVL
SEIDRFNMHK QCQVAVMPLG TGNDLARVLG WGSSCDDDTH LPQILERYES ASTKMLDRWS
IMVFEKAITV PKMPKMSITT EQEALLTGMV TSANHHLRFI VETNDTQTLI SSTRSLCDTV
DELVSRICEH HKDDEQLAMK CDILRQKLTM LLDALQEEEL GTHSGDDLVA TIRSLISRSG
PLTTARPSFL NPNISIEKTE KDNINSKERR NSRSLRSSEK EALQCRANSV KRAIYNVVEH
SEPGRPKRYQ RKLSITPFEA LKIPITNSGD STPCGSPLPI IPPINIISPT METSRLTCIS
PLPDTRRDSV DENFFNSINL PAPRQFADSR RSSGVPEVIQ EMEEGASGET VYRVGRLSLS
GGANIDDAGN RLSPSSEAGE NTPTERKVDF LRVPIMTSEP IVDPLSNYRP IEVFERTYYM
AREMDKDKER TASGQVESEK EEADVNEKSE PQEPHRALVH TCNLQVPGIV VTPQSQNVYT
SENFTIIDTD AQTNTEQSSS EDLGGEASDV LSAISNEECS VASEIFDKPE SGHSLGDIIQ
NLDANNFTHI DSPETSDETE PMPGESLMDD ISSVLGHDIT NALQDNTITD DTTTLCSEHA
GPTKPPRKKS LSALVQSKTH PRRRNSSPPR KAGLARMDSD DNPQQFGFEN IVFEIDNRCD
DQKIREPPRY CSLAQFVEGN DIARQSFKQL MLDRNSGDNH NDNGKNEEAD TPTNSAPTRT
YRNLTTTTTS DELETAIKIE INNATTNTTT STSSSISTTT TTSTTSTVKP LESAMASSTS
PTKKSGHGQE ISVVVRPPTP LRGDSVKPTA SSASSASLLA TSSSLLGVRT LNSSEIRRHS
SHAPSLAVRD YDKDKDRRHS GFNPNFLTLD PEHARFLSSS PAASRRISCG SLFKKRNQKL
NVKRTYGLFS VRFFVVAEPD IRLATLALIR PLIPLPNEAL PNLQTLKGSK SSLFMGSTLF
GFEHFSAGDK DEKPGKDKER TPTEETNRKL PIINPIVRLP NWPNLANGTG FISKCLMANA
DTLCAAVSPL MDPDETLLAG YHEKCVMNNY FGIGIDAKIS LDFHNKREEH PEKCRSRARN
YMWYGVLGSK QLLQKTCKNL EQRVQLECDG QRIPLPELQG IVILNIPSFM GGTNFWGNSS
KKEDIFLPPS FDDRVLEVVA VFGSVQMAAS RLINLQHHRI AQCQSVQINI LGDEEIPIQV
DGEAWLQPPG MIRILHKNRV QMLCRNRSLE VSLKTWQEKQ RQHSISIQRD TSSTASEHAV
STDEVISERE CYVLLNFIEA VSSLVKWVKF LIISHPALQH DLYEVACRAS EALESIHPQG
KLLEGPSLRT KLVEVIDSSR QLYDDACTLL RDRGHSLILR EDLETKLSAA LANMEMELKK
CSVQKCIDGK LRAYFNVLAP NEEPDGRRKS RPFWVRLRSG STAGQQQFKP PITNTREAAN
NWSVNEVVTW LETMQLSEYV DSFLKNDIRG KELLTLGRRD LKDLGVVKVG HVKRILQAIK
DLSEN
