ID A0A093NFV0_PYGAD Unreviewed; 1166 AA.
AC A0A093NFV0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=AS28_07424 {ECO:0000313|EMBL:KFW60900.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW60900.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW60900.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW60900.1};
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; KL224531; KFW60900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093NFV0; -.
DR STRING; 9238.A0A093NFV0; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000054081; 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|RuleBase:RU361128};
KW Kinase {ECO:0000256|RuleBase:RU361128, ECO:0000313|EMBL:KFW60900.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW Reference proteome {ECO:0000313|Proteomes:UP000054081};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {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 1097..1160
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 503..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW60900.1"
FT NON_TER 1166
FT /evidence="ECO:0000313|EMBL:KFW60900.1"
SQ SEQUENCE 1166 AA; 130371 MW; D75A5E1313F85754 CRC64;
TIIKEGMLMK 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 VFVAKKGKAY EKATESSEES
EVMARKCSVL KEKLDSLLKT LNDESQASSS LPNPPPTIAE ETEDGDGSGS ACDSSSDRSV
GSSCTARPQI FRPREQLMLR ANSLKKAIRQ IIEHAEKAVD EQNAQTQEQE GFLLSLSASE
EGKELRNEDK ISLQSSHSSS YGVSKGRSQR KASKSPCERL INKGSLSLGS SASLPPQTGN
RDNLPMLNTK ILYPNIRAGM SGSLPGSSVI SRLLIHADPF NSEPENLECY TEKCVMNNYF
GIGLDAKISL DFNNKRDEHP EKCRSRTKNM MWYGVLGTKE LLHRTYKNLE QKVLLECDGR
PIPLPSLQGI AVLNIPSYAG GTNFWGGTKE DDTFTAPSFD DKILEVVAVF GSMQMAVSRV
INLQHHRIAQ CRTVKIAILG EEGVPVQVDG EAWIQPPGYI WIVHKNRAQT LTRDRAFEST
LKSWEDKQKC ELSRPSSFSL QPEIMSEEES TQINHFGQAA GALIHSIREI AQSCQDMEQE
LAHAVNASSK SMDKVYAKSK STEGLNCSLV VEMVNNVKAL HNETELLLAG KMALQLDPPQ
KEQLQAALAD MDLQLRKLAD IPWLWQLMEP CDEENQMLDY SKRSRSGKFR LVTKFKKEKN
NKNKETHSSM GLPVHLWGTE EVAAWLEHLS LCEYKDIFIR HDVRGSELLH LERRDLKDLG
VTKVGHMKRI LHGIKELSRS TPASEV
//