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Database: UniProt
Entry: C1ED05_MICCC
LinkDB: C1ED05_MICCC
Original site: C1ED05_MICCC 
ID   C1ED05_MICCC            Unreviewed;       590 AA.
AC   C1ED05;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=MICPUN_50666 {ECO:0000313|EMBL:ACO65671.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO65671.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO65671.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
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; CP001329; ACO65671.1; -; Genomic_DNA.
DR   RefSeq; XP_002504413.1; XM_002504367.1.
DR   AlphaFoldDB; C1ED05; -.
DR   STRING; 296587.C1ED05; -.
DR   GeneID; 8246604; -.
DR   KEGG; mis:MICPUN_50666; -.
DR   eggNOG; KOG0782; Eukaryota.
DR   eggNOG; KOG1169; Eukaryota.
DR   InParanoid; C1ED05; -.
DR   OrthoDB; 4642163at2759; -.
DR   Proteomes; UP000002009; Chromosome 9.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 2.60.200.40; -; 2.
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:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR   Pfam; PF00609; DAGK_acc; 2.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128}.
FT   DOMAIN          95..235
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  65067 MW;  45BDA9C1F343BAB0 CRC64;
     MSVLAAATVS AAPRAVPSRP ARRRARALRV TSRAREDSPS QSPASARLGT RGPSFHRAVS
     LESPASSSKN DDDDAAPLDV PETTNAVPSD IGQTGQWPPL LVFVNGKSGG RRGEALRESL
     IARKDLNALA CVDLTMPGAS PTPALKEYVG KVPDLRVLVC GGDGTVAWVL QALEELTEIE
     HKPPVGILPL GTGNDLARVF GWGGRYDDAL VKRLSKALKT AEPALLDRWE CKIERRSEAL
     TPGVEPFGQE GSVIFQNYLG VGVDAAAALK FHRARDANPR MFFSAASNKL MYGLFGAYDF
     VFHSHRDLRE QVRVIADGEE VDLPRDAEGV ILLNINSYAG GEFIFIFVWA IRLTWFFLTG
     VKMWEKGKRG RFRNWLGSWL SGGYGDSTEE RWDLSKNIGP GSNPTGDGLD DEFKEKPKKL
     SVREKVRAVW RRRKAKRAAA RLQRSFGKSR KADGLVDVVV VYGALHLGQL SWGTDRPVRI
     CQARHVRLET KRTLPVQADG QPWEQPASVF DVSLRNRATM LRAPRGHPGY GAATWQSTLP
     TPTRAASEAA LRNVAEWLDD RPARDGEVRF GWETWEDPFF DDADSRLDVL
//
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