ID A0A182FR29_ANOAL Unreviewed; 1457 AA.
AC A0A182FR29;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
OS Anopheles albimanus (New world malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB009004-PA, ECO:0000313|Proteomes:UP000069272};
RN [1] {ECO:0000313|EnsemblMetazoa:AALB009004-PA}
RP IDENTIFICATION.
RC STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB009004-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001383,
CC ECO:0000256|RuleBase:RU361128};
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR STRING; 7167.A0A182FR29; -.
DR EnsemblMetazoa; AALB009004-RA; AALB009004-PA; AALB009004.
DR VEuPathDB; VectorBase:AALB009004; -.
DR VEuPathDB; VectorBase:AALB20_037435; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000069272; Chromosome 2R.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd20803; C1_DGKtheta_typeV_rpt1; 1.
DR CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1.
DR CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1.
DR CDD; cd17111; RA1_DAGK-theta; 1.
DR CDD; cd01783; RA2_DAGK-theta; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
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; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00788; RA; 2.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00314; RA; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 3.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 1457 AA; 163231 MW; E591BE168EF5C989 CRC64;
MATGSEHTFG RKTFHKPTYC HHCSDLLWGL IGQGYICEVC NFIVHEKCVS NIVTPCLGIA
PYLIRNPVAH CWSEPSHHKR KFCSVCRKRL DETPAVHCLI CEYFAHVECQ DFAIPDCKEN
ATYVPGKELG HVKHQHHWRE GNLPQSSKCA YCKKTCWSYE CLTGYRCEWC GTTTHGGCRN
NIQAECTFGT LQPIYLPPHA VSIPRTEVPM EAIIGVQNRN KGTPGIQRDY SCPELWTIGM
YEPEYGSNGS TELLLHSVEQ EERKHSADQL SPVSCFTFYD DDDTSVTRGE TDAAASLTAN
SQDKQQQQES GKQQQQQQQQ QYHSDNSLLL ETNDEWAMRP ARSRNLIHPA LRRTKATATD
STLVMRSRSF QDQSDSIPKR LAKAASYSPR FLARFRYRKK HSHQAPPSLY RRSPSPEDGI
TNGGSGSIGG PIRAALAPML LLHTSAPTTR PTSPLVTVSG VENGDEQMQQ QQQQQQQTAT
HVSDIGRSAS FDGGCSSSSS RTGSATVPGV QPTAARTPSV AIYGHQLTVG CPGAVGRCPL
DPRRVASYDD VSEFTFIDDN DDDDDDGEGD DGIADATVVG VVEVEENASN SSTSLLLMRS
VPIATANRSS CSTTTTSRSR SKQIEVNEST VEAWDDGTEP PSVGLHQQLH RQHPIQQQLL
LHPHHHHHPH HHHHLLGRIY RQMRKCSMGW SKTRCRVRRA RSISEEITIE NRYRDDEYVP
KGESSSSGTH PKPDSAHKPD KDKDKKDKEK EERDEETIKV FDGNCSYRRR IFRAITVPRT
CTLEQLLTTA LRAFHIARDS NLFFLTDVYG DEARLQDPTP VPTLHRVEGK RPAIYLRFRD
KENDHGFVRV YPGKLQVENA YVIIPVDNDT TVKDLICEAL KKFGLQSHQI EDYRCSEILL
DRGVTERVLS WNERPWEIMK QLGKDSIRQM ELMRFYLQLK QDPHGPNLAL FVGNLPPGLS
QRNYEHILTE FLGFENKFSS IGPIYYEYGS LVITYENASK AVRAFQALRE SKYEEKHLLV
LLLPNIEPSM VPPGVQPLLV FVNVKSGGCQ GLELISSFRK LLNPYQVFDL DNGGPLPGLY
VFRHIQDYKI LVCGGDGTIG WVLQCLDNVG QDSECSSPPC AIVPLGTGND LARVLRWGAG
YTGGEDPLNL LRDVIDAEEI RLDRWTVVFH PEDKPEDATP KAQPNSTGKK KKIQQQQQQT
QQQQQNQQHH HPSVAIVAAN PAQVVGGAQS EDNSQIFVMN NYFGIGIDAD LCLDFHNARE
ENPNKFNSRL HNKGVYVKMG LRKMVGRKMV KELHKELRLE VDGKVVELPP VEGIIILNIL
SWGSGANPWG PEKEDQFSKP NHWDGMLEVV GVTGVVHLGQ IQSGLRSAMR IAQGGHIKIH
LHSDIPVQVD GEPWVQSPGD VVVLKSALKA TMLKKMKGKM KRRNTEPTMQ VMGPSGIQMT
LAAPQEPDEV DSNNTDF
//
