ID A0A099ZXW4_CHAVO Unreviewed; 830 AA.
AC A0A099ZXW4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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};
DE Flags: Fragment;
GN ORFNames=N301_13355 {ECO:0000313|EMBL:KGL86532.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL86532.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL86532.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL86532.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00023371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000256|ARBA:ARBA00023371};
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|RuleBase:RU361128};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005175}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR EMBL; KL869929; KGL86532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099ZXW4; -.
DR STRING; 50402.A0A099ZXW4; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000053858; 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:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
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; 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; -; 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; 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; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00314; RA; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
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; 2.
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 Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
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:UP000053858};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 31..78
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 93..144
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 302..401
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 491..628
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 182..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL86532.1"
FT NON_TER 830
FT /evidence="ECO:0000313|EMBL:KGL86532.1"
SQ SEQUENCE 830 AA; 92848 MW; E81D5BB9507D8696 CRC64;
VCNFMSHEKC LKNVKIPCSC IAPSLVRVPV AHCFGPPGHY KRKFCTVCRK SLESPAFRCE
VCELHVHTDC ILFACSDCRQ CHQDGHQDHD TYHHHWREGN LSSSARCEVC KKTCGSSEVL
SGMRCEWCGI LAHAACYIIV TPECTFGRLR NMILPPSCVQ LFSRNFSKLH CFRISENLQT
ESDEDDDVDG STQGSAKDVQ ISTDSSKQTL KIFDGNDAVK RNQFRLISVP RIAKNEEVVE
AALRAYYIND DQQEYELQTF TQQALLSDDV INRNDAAEDS NLGSVFRESV PEAWIIRAKP
KDEEVIRIYP AWLKVGMAYV SLRVNKDSTT QTVIKEVLPL LGRQMECLQN FKLVEVLMGS
KQVQRMVLDN QELILNRLKD IRKTSIRQMN QTRFYIVENS KSIVRVNLFV GGLPPQLSPE
EYTNILKDEL AIKTNVVSVS HVYQAQGAVV LEISCFSEAE RIYMLVKDTT VNDKPLNAVV
IPEVMASKIP RNCCPLLVFV NPKSGGLKGR DLLYSFRKLL NPHQVFELTN GGPLPGFHTF
SKVPSFRVLV CGGDGTVGWV LGALEEIRHK LVCSEPSVAI LPLGTGNDLG RVLRWGAGYS
GEDPYSILVS VDEADDVLMD RWTILLDAEE PAEGAENGIA EPEPPKIVQM NNYCGLGIDA
ELSLDFHHAR EEEPGKFNSR FHNKGVYVKV GLQKISHTRN LHRDIKLQVD QHEVELPSIE
GLIFINIPSW GSGADLWGSE SDNRFEKPRI DDGLLEVVGV TGVVHMGQVQ GGFRSGIRIA
QGSYFRVTLL KPIPVQVDGE PWIQAPGQII ISAAGPKVHM LKKSKQKQKK
//
