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Database: UniProt
Entry: A0A0N1PD11_LEPSE
LinkDB: A0A0N1PD11_LEPSE
Original site: A0A0N1PD11_LEPSE 
ID   A0A0N1PD11_LEPSE        Unreviewed;       447 AA.
AC   A0A0N1PD11;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=ABL78_4653 {ECO:0000313|EMBL:KPI86270.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI86270.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI86270.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI86270.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA   Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA   Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT   Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT   donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI86270.1}.
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DR   EMBL; LJSK01000139; KPI86270.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1PD11; -.
DR   EnsemblProtists; KPI86270; KPI86270; ABL78_4653.
DR   VEuPathDB; TriTrypDB:Lsey_0139_0010; -.
DR   OMA; EWRNAYM; -.
DR   OrthoDB; 4642163at2759; -.
DR   Proteomes; UP000038009; 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: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; -; 1.
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   Pfam; PF00609; DAGK_acc; 1.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361128};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128}.
FT   DOMAIN          60..164
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          169..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  48591 MW;  43652772E9BD3667 CRC64;
     MADHSTNNKS LTSEPERPCA FVNMNSGERS AALFVADQLK KNFGADNVLD LFPVKGKPPV
     IEEAKQFLIQ RKPDLLVVAG GDGTVSLGFD IVDEVRAAKL VGPATAPIAV IPMGTGNDLS
     RSLGFGGGYK KPLVKAEERF TKVIKRLFMA RPRVIDRFAL TITTIDPDTV TPGHAGGVNG
     HRPSKQRSAP SLPKEECRSF LEERHRCSHA ESAASSAEQR QQQHQQESSS PTPAQPPSSR
     CKETKKVFTN YFSIGFDAEV AKAFGDFRDH HPGICKSRVG NKIWYGCFGC NAMCCSSTLP
     KKHVSLTVDG KAIKVPSNMK SIVVSSMITY AGGNILWADS RQKFDTQAVD DGKVEVVALE
     GVWHMVGIGT RIRSGKKLAQ GSSIVLYSPA HFTMQYDGEP IAAMGAPDQM VKIVIEFMSQ
     SLGTEVPLEK ESNRKATQAS HSETERK
//
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