ID A0A091GPI6_BUCRH Unreviewed; 1164 AA.
AC A0A091GPI6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=N320_00914 {ECO:0000313|EMBL:KFO85069.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO85069.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO85069.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO85069.1};
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; KL506608; KFO85069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GPI6; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000054064; 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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
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; cd20847; C1_DGKdelta_rpt1; 1.
DR CDD; cd20893; C1_DGKdelta_rpt2; 1.
DR CDD; cd13274; PH_DGK_type2; 1.
DR CDD; cd09575; SAM_DGK-delta; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR047478; C1_DGKdelta_rpt1.
DR InterPro; IPR047477; C1_DGKdelta_rpt2.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR037606; DGK-delta_SAM.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF30; DIACYLGLYCEROL KINASE DELTA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Reference proteome {ECO:0000313|Proteomes:UP000054064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..94
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 111..161
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 183..234
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 265..400
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT DOMAIN 1095..1158
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 500..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO85069.1"
FT NON_TER 1164
FT /evidence="ECO:0000313|EMBL:KFO85069.1"
SQ SEQUENCE 1164 AA; 130186 MW; CA8F3E18BC13D798 CRC64;
TVIKEGMLMK QTSSFQRWKR RYFKLRGRTL YYAKTAKSII FDEVDLTDAS VAESSTKNVN
NSFTIITPCR KLILCADNRK EMEDWIAALK TVQNREHFES TQYSMDHFSG MHNWYACSHA
RPTYCNVCRE ALSGVTSHGL SCEVCKFKAH KRCAVRATNN CKWTTLASIG KDIIEDEDGI
SMPHQWLEGN LPVSAKCTVC DKTCGSVLRL QDWRCLWCKA MVHTACKELL PNKCPLGLCK
VSVIPPTALN SIDSDGFWKA TCPPSCTSPL LVFVNSKSGD NQGVKFLRRF KQLLNPAQVF
DLMNGGPHLG LRLFQKFDTF RILVCGGDGS VGWVLSEIDS LNLHKQCQLG VLPLGTGNDL
ARVLGWGSAC DDDTQLPQIL EKLERASTKM LDRWSIMVYE TKLPRQASTS TVTEDFSEDS
EKILFYEDSV AAHLSKILTS DQHSVVISSA KVLCETVKDF VARVGKAYEK ATESSEESEV
MARKCSVLKE KLDSLLKTLN DESQASSSLP NPPPTIAEET EDGDGPGSAC DSSSDRSVGS
SCTARPQIFR PREQLMLRAN SLKKAIRQII EHAEKAVDEQ NAQTQEQEGF LLSLSASEEG
KELRNEDKIS LQSSHSSSYG VSKGRSQRKA SKSPCERLIN KGSLSLGSSA SLPPQTGNRD
NLPMLNTKIL YPNIRAGMSG SLPGSSVISR LLIHADPFNS EPENLECYTE KCVMNNYFGI
GLDAKISLDF NNKRDEHPEK CRSRTKNMMW YGVLGTKELL HRTYKNLEQK VLLECDGRPI
PLPSLQGIAV LNIPSYAGGT NFWGGTKEDD TFTAPSFDDK ILEVVAVFGS MQMAVSRVIN
LQHHRIAQCR TVKIAILGEE GVPVQVDGEA WIQPPGYIWI VHKNRAQTLT RDRAFESTLK
SWEDKQKCEL SRPSSFSLQP EIMSEEESTQ INQFGQTAGA LIHSIREIAQ SYQDMEQELA
HAVNASSKSM DKVYAKSKST EGLNCSLVVE MVNNVKALHN ETELLLAGKM ALQLDPPQKE
QLQAALADMD LQLRKLADIP WLWQLMEPCD EENQMLDYSK RSRSGKFRLV TKFKKEKNNK
NKETHSSMGL PVHLWGTEEV AAWLEHLSLC EYKDIFIRHD VRGSELLHLE RRDLKDLGVT
KVGHMKRILH GIKELSRSTP ASDV
//
