ID A0A091K223_COLST Unreviewed; 894 AA.
AC A0A091K223;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=N325_01799 {ECO:0000313|EMBL:KFP31055.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP31055.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP31055.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP31055.1};
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=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000256|ARBA:ARBA00023400};
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; KK541693; KFP31055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091K223; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000053615; 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; cd20849; C1_DGKzeta_rpt1; 1.
DR CDD; cd20895; C1_DGKzeta_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR047485; C1_DGKzeta_rpt1.
DR InterPro; IPR047484; C1_DGKzeta_rpt2.
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 PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF43; DIACYLGLYCEROL KINASE ZETA; 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; SM00109; C1; 2.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
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:UP000053615};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 239..373
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 787..810
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 823..855
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 199..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..217
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP31055.1"
FT NON_TER 894
FT /evidence="ECO:0000313|EMBL:KFP31055.1"
SQ SEQUENCE 894 AA; 100357 MW; D0F203A40A43A891 CRC64;
RKAIAKSSLQ HMVAQPNPAV ALRSDSERQI RSTVDWSETA VYGEHIWFEA NVSGDFCYVG
EQNCMAKLLQ KPLSRRKCAA CKIVVHTPCI EQLEKINFRC KPSFRESGSR NVREPIVVRH
HWVHRRRQEG KCRQCGKGFQ QKFAFHSKEI VAISCSWCKQ AYHSKVSCFM LQHIEEPCSL
GAHAAVVVPP TWILRVRRPQ NPLKSSKKKK RTSFKRKSSK KGAEEGRWKP FVIKPTPAPL
MKPLLVFVNP KSGGNQGAKI IQSFMWYLNP RQVFDLSQGG PKEALELYRK VHNLRILACG
GDGTVGWILS ILDQLRLNPP PPVAILPLGT GNDLARTLNW GGGYTDEPLS KILSHVEDGN
IVQLDRWNLH VEPNPEASPE EKDEAAADKL PLDVFNNYFS LGFDARVTLE FHESREANPE
KFNSRFRNKM FYAGTAFSDF LTGSSKDLAK HVRLVCDGTD LTSKIQDLKP QCLVFLNIPR
YCAGTMPWGN PGEHHDFEPQ RHDDGCIEVI GFTMTSLAAL QVGGHGERLC QCRQVLLSTS
KAIPMQVDGE PCKLAASCIH ISLRNQANMV QKTKRRNSVP LLNDQQPVPE RLRIRVSRIS
MRDYEALHYD KEKLKEASVP LGIIVVPGDS DLELCRTQIE RLQEEGDGAK PKTLSSQKLS
PKWCFLDSTT ADRFYRIDRA QEHLNYVTEI SQDELYVLDP ELVITQTVGT SPAMPDLVDT
SAAPTGHHFA FPSSSSTPPS SPALGAEPER CLPHRDDLLI EAAKSGNFSE FQELHRAGRD
LMVRDSSGQT VLHHAVKSGS KDMVKYIIEN APSEILDATE EENGETSLHQ AAALRQRTIC
HYIVEAGASL MKTDLQGDTP KHRAEKAKDP DLAAYLESRQ HYQMIQREDQ ETAV
//
