ID   A0A3Q4GML1_NEOBR        Unreviewed;       731 AA.
AC   A0A3Q4GML1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   08-MAY-2019, entry version 2.
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};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000008003};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000008003}
RP   NUCLEOTIDE SEQUENCE.
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNBRP00000008003}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J.,
RA   Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J.,
RA   Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A.,
RA   Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O.,
RA   Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R.,
RA   Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T.,
RA   Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S.,
RA   Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D.,
RA   Rakotomanga M., Renn S.C.P., Ribeiro F.J., Ron M., Salzburger W.,
RA   Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R.,
RA   Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D.,
RA   Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A.,
RA   Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid
RT   fish.";
RL   Nature 513:375-381(2014).
RN   [3] {ECO:0000313|Ensembl:ENSNBRP00000008003}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2019) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-
CC         3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107;
CC         Evidence={ECO:0000256|RuleBase:RU361128};
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC       family. {ECO:0000256|RuleBase:RU361128}.
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DR   RefSeq; XP_006794133.1; XM_006794070.1.
DR   Ensembl; ENSNBRT00000008226; ENSNBRP00000008003; ENSNBRG00000006079.
DR   GeneID; 102798251; -.
DR   GeneTree; ENSGT00940000157144; -.
DR   CDD; cd00029; C1; 1.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.238.110; -; 1.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR029477; DAG_kinase_typeI_N.
DR   InterPro; IPR037607; DGK.
DR   InterPro; IPR038199; DGK_typeI_N_sf.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   PANTHER; PTHR11255; PTHR11255; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF14513; DAG_kinase_N; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   SUPFAM; SSF47473; SSF47473; 2.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
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   Calcium {ECO:0000256|PROSITE-ProRule:PRU00448};
KW   Kinase {ECO:0000256|RuleBase:RU361128};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW   Transferase {ECO:0000256|RuleBase:RU361128}.
FT   DOMAIN      113    148       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   DOMAIN      158    193       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   DOMAIN      207    257       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      272    322       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      376    510       DAGKc. {ECO:0000259|PROSITE:PS50146}.
FT   CA_BIND     126    137       {ECO:0000256|PROSITE-ProRule:PRU00448}.
FT   CA_BIND     171    182       {ECO:0000256|PROSITE-ProRule:PRU00448}.
SQ   SEQUENCE   731 AA;  81944 MW;  B0B1B991C30C47E4 CRC64;
     MSSPTNPEVK ELNPVDFIQL QQYIEYNNLK VKDVLREFYA DGSLARHRHG ECINEEGFRL
     FLKTYLEVED FPVDLCQRLF RSFQNSEPGQ EDSTKEVFLK DVSCYFSLLE DGQPRDKLEF
     AFRLYDRDGN GVLDSSEVDR IIAQMMHAAE YLDWDVSELK PVLKDMMTAI DADSSGTVSL
     DEWVQGGMNN VPLLVLLGLK MTQKDGQHLW RMKNFNKPVY CNVCHSMLLG LRKQGLCCTS
     CKYTVHGRCA NKNPAPCART YVKSKKEIGV STHDWVSGNC DSRKCDKCQK KIKSLQGLTG
     KHCVWCHTMR HDQCVDQEST QCTCGLLRDH ILPPWAIYPV IKERPNNVKN GCSGSGDDSE
     LNTTPDGQVL QICPVLNAHP LLVFVNPKSG GKQGERVLRK FQFLLNPRQV YNLSNGGPGP
     GLSFFRNLKE YRILVCGGDG TVGWILDAID KGNLLVRPPV AVLPLGTGND LARCLRWGGG
     YDGEDLNRIL KDIEGSSQVL MDRWSVQVIT DENQEEGDPV PYEIINNYFS IGVDASIAHR
     FHTMREKHPQ KFNSRMKNKL WYFEFATSET ISASCKKLSE NLTIECCGTA LDLSGVSLEG
     VAILNIPSMH GGSNLWGETK KVDTKGLTAQ EEPEVIVNPE ILKVTSQDLS DRRLEVVGLE
     GAMEMGQIYT GLKSAVRLAK TSQITIRTKK ALPMQIDGEP WMQPPCTIQI THKNQACMLM
     GPPAKPSGFF K
//