ID A7SDC5_NEMVE Unreviewed; 957 AA.
AC A7SDC5;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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};
GN ORFNames=NEMVEDRAFT_v1g244480 {ECO:0000313|EMBL:EDO38287.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO38287.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO38287.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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 -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR EMBL; DS469629; EDO38287.1; -; Genomic_DNA.
DR RefSeq; XP_001630350.1; XM_001630300.1.
DR AlphaFoldDB; A7SDC5; -.
DR STRING; 45351.A7SDC5; -.
DR EnsemblMetazoa; EDO38287; EDO38287; NEMVEDRAFT_v1g244480.
DR eggNOG; KOG0782; Eukaryota.
DR HOGENOM; CLU_003770_4_0_1; -.
DR InParanoid; A7SDC5; -.
DR OMA; NMIDNDK; -.
DR PhylomeDB; A7SDC5; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IBA:GO_Central.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IBA:GO_Central.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd20802; C1_DGK_typeIV_rpt1; 1.
DR Gene3D; 2.60.200.40; -; 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; IPR037607; DGK.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF114; EYE-SPECIFIC DIACYLGLYCEROL KINASE; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 3.
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; 2.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128}.
FT DOMAIN 288..423
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 850..873
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 886..918
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 107765 MW; D6F00B00D9602733 CRC64;
MAAKPGNFRE NTLGVEHVGG SEDGGNASKL TRGTAKSRSY KQAVGNHHDY HSPSTSNNDT
NANHVEEKNQ NPCTDSDVCD WTDNAINGKH MWVDSEASGT LCYLYDFDCV DNAINGKHMW
VDSEASGTLC YLYDFDCVKS GARKKCTACK IVIHTKCMEK LERINFICKT TFREIQPKGV
HESNMRHHWV HRRRQDGRCE TCGKSFQHML SFQSKYHNKD ECFKVDRIEE LCDLGVHSNV
IVPPSWVVKI PKKARSFPTK RNSFKKKSIK RRSTKERKPF VIKPSGSANK RPLVVFINPK
SGGNQGLRIM HKFQWLLNPR QVFDLSREGP REGLELYRKV PNVRLLACGG DGTVGWILSE
LDKLKFNPRP PVAILPLGTG NDLSRALNWG GGYADEPLSK ILTHVDEGSV VQLDRWDLEV
VPSGYTDGEI AESRLPLNVM NNYFSLGFDA EVCLEFHESR EAHPAKFNSR VKNKLFYGKA
SSTTFIQGKA KDFYKHTKLE CDGVDITEKL LEAKPMCLLF LNISKYSAGT SPWGNPGRDH
EFLPQRSDDG YIEVLALTSA TLATTRVGGH GERLAQCRNV IMTTSKSIPM QVDGEPCRLQ
PSRIRISVRN QADMIQKVKR RALGSSGESE PAPSPEPVKV KIFCVNFKDY ELHCYDIRRL
RESATVLTTT SIEPDADLEQ MRVWIERFIS EEEESQKTIL SDDWCFLDTS YPDRVYRVDV
AQENIYNVVD IVEKGVFIVD LKGGKTVTRT SSSTTPPTSV NLARRGLPVA HSQESLREDS
DDVLQTSLIT PFTPTGKKEF VIPAEDEVWV KNTTAKKNDL LMIEAAKTGE LEKVIELHEA
GVSLTVGDLR GWRPLHYAAR HGHKSIITYI ISNVPRCVLD LVEEEKGQTA LHKAAFYQRR
TICSLLVQAG ASLTRTDYDG NTPRIQALKC QDKELSRYLE TQEHLQIVAA EDYETAV
//
