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DGKH_DROYA
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   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=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   STRING; 7245.FBpp0269956; -.
DR   PRIDE; B4PRE2; -.
DR   GeneID; 6536003; -.
DR   eggNOG; KOG1170; Eukaryota.
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: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; 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
 
 
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