DGKH_DROSI
ID DGKH_DROSI Reviewed; 1905 AA.
AC B4R0A5;
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=GD19954;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000312|EMBL:EDX12030.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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=EDX12030.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000364; EDX12030.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B4R0A5; -.
DR SMR; B4R0A5; -.
DR STRING; 7240.B4R0A5; -.
DR Proteomes; UP000000304; 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: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..1905
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000375990"
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 1842..1905
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 1005..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1386
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 1164..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1905 AA; 212678 MW; EB292E228AD94D66 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 ENTPTERKVD FLRVPIHTGE PIVDPLCDYR PHEVFEQKEN
DKEKDKPVEI DMERDTCVEK DGSVPEEKLV HTCNIQVPGV VVTPNPQNVY SSASITIIDT
DAQTTTEQSS SDDLGGEASD VLSAISNEEC SVASEIFDKQ DAGQTVGDII QNMDASNFTH
IDSPETSDET EAMPGESIMD DISSVLGHDI TYALQDNTLT DDTTTLCSEH VGPPKPPRKK
SLSALSRTQA HPRRRNSSPP RIARLARMDS DDNPQQFGFE NIVFEIDNRC DDQKMREPPR
YCSLAQFVEG NDIARQSFKQ LMLEQHRGED NDSEYPEHQQ TPTNKGANLL ATTSEDELST
QTAIKIEIQD IDATVRNLNS SMKPNTILTT STSPTKKSGH GQDISVVVRP PTPLRGDSIK
PTVSLLPVSS GGAMAVSMTC SGMLGVRAMN ASEIRRHSSH APGLAVREFD KDKDRRHSGF
NPNQLTLDPE HARFLSSSPA ASRRISCGSL FKVKNKKIAT KRSYGLFSVR FFVVAEPDFR
LATLALIRPL IPLPNEALPN LQTLKGSKSS LFMGSTLFGF DHLASAERDK EEKGGKDKEK
TPTEETNRKL PIINPLVRLP NWPNLANGGG FISKCLLANA DTLCAAVSPL MDPDETLLAG
YHEKCVMNNY FGIGIDAKIS LDFHNKREEH PEKCRSRARN YMWYGVLGSK QLLQKTCKNL
EQRVQLECDG QRIPLPELQG IVILNIPSFM GGTNFWGSST KKDDIFLPPS FDDRVLEVVA
VFGSVQMAAS RLINLQHHRI AQCQSVQINI LGDEEIPIQV DGEAWLQPPG MIRILHKNRV
QMLCRNRSLE LSLKSWQEKQ RQHSISIQRD ASSTASEHAN STDEVISERE CYVLLNFIEA
VSSLVKWVKF LIISHPALQH DLYEVACRAS EALESIHPQG KLLEGPSLRT KLVEVIDSSR
QLYDDACTLL RDRGHSLILR EDLETKLSAA LANMEMELKK CSVQKCIDGK LRAYFNVLAP
NEEVDGRRKS RPFWVRLRSG STAGQQQFKP PMTNTREAAN NWSVNEVVTW LETMQLSEYV
DSFLKNDIRG KELLTLGRRD LKDLGVVKVG HVKRILQAIK DLSEN
