ID B0WJD5_CULQU Unreviewed; 1334 AA.
AC B0WJD5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 105.
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};
GN Name=6039164 {ECO:0000313|EnsemblMetazoa:CPIJ007371-PA};
GN ORFNames=CpipJ_CPIJ007371 {ECO:0000313|EMBL:EDS29110.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS29110.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS29110.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ007371-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ007371-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) 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 EMBL; DS231959; EDS29110.1; -; Genomic_DNA.
DR RefSeq; XP_001848820.1; XM_001848768.1.
DR STRING; 7176.B0WJD5; -.
DR EnsemblMetazoa; CPIJ007371-RA; CPIJ007371-PA; CPIJ007371.
DR KEGG; cqu:CpipJ_CPIJ007371; -.
DR VEuPathDB; VectorBase:CPIJ007371; -.
DR VEuPathDB; VectorBase:CQUJHB016099; -.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_003770_0_0_1; -.
DR InParanoid; B0WJD5; -.
DR OMA; GFHHARE; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; IPR000504; RRM_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; PS50102; RRM; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 69..119
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 132..180
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 198..249
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 731..829
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 835..912
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 920..1058
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 28..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..518
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1334 AA; 147972 MW; 0083A95EDB8DE72C CRC64;
MDEEALAAVS AVVTWSRPSL AGGVASSSRL LAPAEQDPQS TTAATPEPEP EAAASHCIAA
AQNKMAGGEH SFGRKTFHKP TYCHHCSDLL WGLIGQGYIC EVCNFIVHEK CVTNVITPCL
GVAPYLIRNP VAHCWSEPTQ HKRKFCSVCR KRLDETPAVH CLICEYFAHV ECQDFAIPDC
KENATYVPGK ELGHVKHQHH WREGNLPQSS KCAYCKKACW SYECLTGYRC EWCGTTTHGG
CRTNLPSECT FGTLQPIYLP PHAVSIPRTE VPMEAIIGVQ NKNKGTPGLP RDYSCPELWT
IGQDFDEPSP PGIVTNGTSA APSPMPYKLP VFTFFDDGDE SESSQPRYPS DTDLLLALED
TPASPFRPVP SRNLIHPAMR KVAATKLGTP KDTVVMRSRS FQDQTDSIPK RLRMLPFLRA
KDRAKKRSPL CSTTDSNVSS GCPSPLPPHK SSCSPVTAAS VTTIQTTDEL LPAVASLRDG
ERRVLSYGDV SSFVFIDEDA ALGGDDEDEE EEEDDDDSSS TAKVVTDAKL NARNVASGCA
VTTSKGDQQA DKENRRTGGG HLLGRIYRRM RKCSMGWSKT GCRERRARSI SEELASDNAR
CSDDLQKAEG SSGSHSSSKP DSAHKSDKDK DKKDKEKEER DEETIKVFDG NCSYRRRIYR
AITVPRTCSL EQLLTTALRA FHIARDSNLF FLTDLYGDEV RLQDPTPVLN LHRVEAKRPA
IYLRFRDREN DHGFVRVYPG KLQVENAYVN VPVHNDTTVK DLLGESLKKF GLEGHQVEDY
RCSEILLDRG VTERVLSWNE RPWEIMKQLG KDSIRQMEMM RFYLQLKQDP HGPNLALFVG
NLPPGLSQRN YEHILTEFLG FENKFSSIGP IYYEYGSLVI TYENASKAVR AFQALRESRY
EDKNLLVLLL PNIEPSMVPS GVQPLLVFVN VKSGGCQGAE LISSFRKLLN PYQVFDLDNG
GPLPGLYVFR HIQDYKILVC GGDGTIGWVL QCLDNVGQDS ECSSPPCAIV PLGTGNDLAR
VLRWGAGYTG GEDPLNLLRD VIDAEEIRLD RWTVVFHPED KPEDAAPKPS TNSAGKKKKI
QQSQQQNQHH HPATTAISAI GSGGTQSEDN SQIFVMNNYF GIGIDADLCL DFHNAREENP
NKFNSRLHNK GVYVKMGLRK MVGRKMIKEL HKELRLEVDG KVVDLPPVEG IIILNILSWG
SGANPWGPEK EDQFSKPNHW DGMLEVVGVT GVVHLGQIQS GLRSAMRIAQ GGHIKIHLHT
DIPVQVDGEP WVQSPGDVVV LKSALKATML KKMKGKMKRR NTEPTMQVMG PSGIQMTLAA
PQEPEEVDSN NTDF
//
