ID A0A091I4R2_CALAN Unreviewed; 830 AA.
AC A0A091I4R2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=N300_12746 {ECO:0000313|EMBL:KFP02433.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP02433.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP02433.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP02433.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL218126; KFP02433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091I4R2; -.
DR STRING; 9244.A0A091I4R2; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000054308; 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:UP000054308};
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 NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP02433.1"
FT NON_TER 830
FT /evidence="ECO:0000313|EMBL:KFP02433.1"
SQ SEQUENCE 830 AA; 92724 MW; A942C4947078D45D CRC64;
VCNFMSHEKC LKNVKIPCSC IAPSLVRVPV AHCFGPPGHY KRKFCTVCRK SLDSPAFRCE
VCELHVHADC ILFGCSDCRQ CHQDGHQDQD TYHHHWREGN LSSSARCEVC KKTCGSSEVL
SGMRCEWCGI LAHAACYIIV TPECTFGRLR NMILPPSCVQ LFSRNFSKLH CFRISENLQT
ETDEDDDVDG LTLGSAKDIQ ISTDSSKQTL KIYDGNDAVK RNQFRLISVP RIAKNEDVVE
AALRAYYIND DHQDYELQTF TQQALLSDDV INRNDAAEDS NLSSVFRESV PEAWIIRAKP
KEEEVIRIYP AWLKVGMAYV SLRVNKDSTT QTVIKEVLPL LGRQTECLQN FKLVEVLMGS
KQVQRMVLDS QELILNRLKD IRKTSVRQMN QTRFYIVENS KSVVRVHLFV GGLPPQLSPD
EYTNILKDEL AIKTNVVSVS HVYQAQGAVV LEISCFSEAE RIYMLVKDTT INDKPLNAVV
LPEVLASKIP QNCCPLLVFV NPKSGGLKGR DLLYSFRKLL NPHQVFELTN GGPLPGFHTF
SKVPSFRVLV CGGDGTVGWV LGALEEIRHK LVCSEPSVAI LPLGTGNDLG RVLRWGAGYS
GEDPYSILVS VDEADDVLMD RWTILLDAEE PAEGGENGLA EPEPPKIVQM NNYCGLGIDA
ELSLDFHHAR EEEPGKFNSR FHNKGVYVKV GLQKISHTRN LHKDIKLQVD QHEVELPSIE
GLIFINIPSW GSGADLWGSD NDNRFEKPRI DDGLLEVVGV TGVVHMGQVQ GGFRSGIRIA
QGSYFRVTLL KPIPVQVDGE PWIQAPGQII ISAAGPKVHM LKKSKQKQKK
//
