ID V9I9X7_APICE Unreviewed; 927 AA.
AC V9I9X7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=ACCB00128.2 {ECO:0000313|EMBL:AEY57099.1};
OS Apis cerana (Indian honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=7461 {ECO:0000313|EMBL:AEY57099.1};
RN [1] {ECO:0000313|EMBL:AEY57099.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:AEY57099.1};
RA Sun L., Zheng H., Wang Y., Xie X., Zhu Y., Gu W., Wang S.;
RT "Decoding the brain transcriptome of the Eastern honeybee (Apis cerana)
RT based on pyrosequencing.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; JR036352; AEY57099.1; -; mRNA.
DR AlphaFoldDB; V9I9X7; -.
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; IPR035979; RBD_domain_sf.
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; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50200; RA; 2.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE 2: Evidence at transcript level;
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 RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 13..63
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 76..124
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 142..193
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 276..364
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 365..463
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 469..546
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 554..692
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 234..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 103651 MW; 8FE0FAC56654C13C CRC64;
MASVSAETPA SHGHSFSKKT FHKPTYCHSC TDMLWGLIQQ GYICEVCNFV VHDRCLKAVV
SPCSSIAASL IKNPVAHCWS EQVHHRRKFC NVCRKRLDDN LSIHCEICEY FAHTECQDFA
VADCKENATY LPGKDLAQVN HTHHWREGNL PSSSKCAVCK KNCFSAECLS GFRCEWCGMT
LHSYCYKNIP QECTFGNLEP IYLPPHAVSI PRTEVPMEAI IGVQVRRKEA LAPRSISEEF
SSGDARYRDN GEPGPGSAHG RDPRSPKEKE DKERGDEEMI KVYDGNNSLR RRIFRVITVP
RQATTEQVLT SALRAFHITK DPSNFYLTDV YATDETELCD PNPVLNLNRK EGKRPAVFLR
FKDSESGEVR VYPGKLQVSE SFCIVPVTEA TTIADLIEEA LQKFGLQNFK SEDYRCSEIL
LDHGVTERVL CRDEKPWEIV KQLGKDSIRQ MELMRFYLQL KQDPHGPNLA LFVGNLPPNL
SERSYENMLT EFLGKENKFS SIGPIYYEYG SMVIIYEDSN KAVTALYTLR ESKYEDKHLL
VMLLPSIEPS MVPPGVQPLL VFVNVKSGGC QGLQLISSFR KLLNPYQVFD LDNGGPLPGL
YVFRHIKDYK ILVCGGDGTI GWVLQCLDNV GQDSECSSPA CAIVPLGTGN DLARVLCWGS
GYTGDEDPLN LLRDVIDAEK SMLDRWTVVC HTEEKEDKQS STNAGGAGAP SEDNTQILVM
NNYFGIGLDA DLCLDFHNAR EENPNKFKSR LRNKGVYVTM GLRKMVKRKP CKDLHKEIRL
EVDGRLVELP QVEGIIILNI LSWGSGANPW GPDVKEDHFQ TPNHGDGMLE VVGVTGVMHL
GQIQSGLRTA MRIAQGGHIK IHLYSDIPVQ VDGEPWIQSP GDIVVLKSAL TATMLKKNKI
KRRNTEPSIP PANGVGGKST DECSNKS
//
