ID T1L4S0_TETUR Unreviewed; 1565 AA.
AC T1L4S0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur40g00260.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur40g00260.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Target cell membrane {ECO:0000256|ARBA:ARBA00004175}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR EMBL; CAEY01001161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 32264.T1L4S0; -.
DR EnsemblMetazoa; tetur40g00260.1; tetur40g00260.1; tetur40g00260.
DR eggNOG; KOG0782; Eukaryota.
DR HOGENOM; CLU_003770_4_2_1; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0044218; C:other organism cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; 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; cd20802; C1_DGK_typeIV_rpt1; 1.
DR CDD; cd20855; C1_DGK_typeIV_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
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 PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF114; EYE-SPECIFIC DIACYLGLYCEROL KINASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Membrane {ECO:0000256|ARBA:ARBA00023298};
KW Neurotoxin {ECO:0000256|ARBA:ARBA00022699};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Presynaptic neurotoxin {ECO:0000256|ARBA:ARBA00023028};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Target cell membrane {ECO:0000256|ARBA:ARBA00022537};
KW Target membrane {ECO:0000256|ARBA:ARBA00023298};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128}.
FT DOMAIN 815..950
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 1460..1492
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1495..1527
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..654
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1565 AA; 170858 MW; EBAC586A750573FD CRC64;
MQRLRDKFRR KNVSTPRVDR SPSGNIATPA TSSGASSHYL NNVLTLDSTS ESYHSLMVPD
SCASTSNDKI DSCGANSFTN SNNLSLPVGV RQIRSASYDE IRIRRDIDSI RLDELGSTTL
STEADPSSLT TEPEVLSSGS EMLDVPLAAK SARSKSFDSA SGKEAMSGKL RSGSSISFLE
IPKWKLFIRR SSSPSSGRAS PFLFFGEKCI HCSLVEEQAA LKALQQTFVS STGSLTTEDD
DTDDEVVATC STRRSFRPRR RSTSDDLNEG EHDHATFSGP FDKNLAKNIL SKCGSSSEPS
SPRDEEETKS DSELISKATG TDSDIVTHVK TARVASDSDA QCLISGDDIS PMVTLSAAPP
PEAPSPLQEF EEDLGNGITV ISLEVPLTKQ NRSASIDASF LKVPENLGSR PKETSPTKTQ
RSHSVDISLP TKPDGPYLIV QSSRPEQIFL KKAIQGEIKI STENGETRTL RSAPDWGETA
INGDHLWVST STSGDLCYVG ENECSKQGPR LCCPACKITA HTGCIGILID KIKFHCKPTF
KDVGVRQYRE QTVIHHHWVH RRSQKGRCRQ CGKSFQSKLS FANKEIVAIS CSWCKTAYHN
KENCFTLERL TETCSLGIHK DLIIPHSWIV KLPRKGSFKS SIRRSPKNKR SSSKRRTKKE
DASPIVAVSS ENSHHLPVHP LSSSSSSCSP QPPPIHPTVG LTSTSTMPPQ SSSAPQPLTP
LSANQLPSCS FSSSAVLSQS QPNNSNPMDI SSSSSLATSS TITATSSTAI SSLGAGPQPN
VPTPPPPGAV PTEPRPSLCA PGQHRSFAIK PIPSPDSKPL LVFINPKSGG NQGSKLMQKF
QWLLNPRQVF DLSQGGPRPG LELYRKVPNL RILACGGDGT AGWILSVLDE IGFKPSPPIA
VLPLGTGNDL ARALGWGGGY TDEPVSKILL NIKDGEVVQL DRWDVKVTRN TDLNLIEQAA
DTPEGAKESL PLNVINNYFS IGVDAHIALE FHEAREAHPE RFNSRLRNKM FYGQAGGKDL
LQRKWKDLVT YITVECDGVD LTQRLRDLKV HSLLFLNIPC YGGGTRPWGS ASPSFELPRT
DDGLIEVIGL TTYQLPLLQA GGHGSCVAQC KEAKIITRRT IPMQVDGEPC RLLPSIIRIK
VKNQANMVAK SKTHCQIASM PTLDREIVIP VRKLNILDYE TFHYDKSRLH DASIVLGKLQ
INPDLELNHV RALIRQMVAN HRKGSTSIHM LNKEPGDEMA RYRLEKAFDI SNDWCFVDSC
TAERYFRIDR AQEHLHYVVD ICNDELYILD PTDNGYDRDK LAKASNVPTT QLADNSPASG
LSGDETPSPV DPALYGDNNN TIVLFKPPTT KEPGSGKDDS GDTLNVNTAS QLLEGSSIPG
TPTTATETLT ETATESNNPS ASKETVMSDK EAVRVNVTGP DNISIDYNSN EIIEAVKRAD
LTSLKRLREQ GYNLSAVDSN GLTTLHYAAM LGYHDIIQYL VDLQPDLINY KTYNDGQTPL
HYAILYGQRI SCFILAAAGS SVTDADAYSH NAKDLAIMKG DHELAAYLDQ FACYQATFNE
RETTV
//
