ID W7ABZ2_9APIC Unreviewed; 1010 AA.
AC W7ABZ2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=C922_00068 {ECO:0000313|EMBL:EUD69205.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD69205.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD69205.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD69205.1,
RC ECO:0000313|Proteomes:UP000030640};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic
CC acid (PA). {ECO:0000256|ARBA:ARBA00002064}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR EMBL; KI965460; EUD69205.1; -; Genomic_DNA.
DR RefSeq; XP_008813907.1; XM_008815685.1.
DR AlphaFoldDB; W7ABZ2; -.
DR EnsemblProtists; EUD69205; EUD69205; C922_00068.
DR GeneID; 20035342; -.
DR VEuPathDB; PlasmoDB:C922_00068; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000030640; 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 PANTHER; PTHR11255:SF34; DIACYLGLYCEROL KINASE ETA; 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 160..248
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 55..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 117099 MW; 1471051AF9E95933 CRC64;
MKYIFLFVNP TSGGNRASMF IDFGVNDIVF HKPHKCHFSI YNILEGEPGK KPGFLHLSSV
TNSPRQDEIK SESVTPNSRG LVSKSTLSVE GKSGSPNRNP SHNSSENGTN EPSNSTGSGG
KTKGEDHHLS GTKKGKNSQK TGSDDSEGTA GEDENIFAYV LVAGGDGTLN WFLKEAEQYD
IKDDKIAVGV IPFGTGNDFA KAFGWKKMDG FFNYTYLFDI LKKIVDQTFK SKIDKHDYWN
VHVVLKENGY FNKISSSTKK KETLTENEQN VKVLKMCMSN YFSIGIDSRI GRGFERHRQK
SAFVNKLIYV VEGFKKIIFK KNIPVNLIID KMVTGKNYDD VIFTTNRNDS TALPAPLLKK
AMSIICVNIP SYSSGNDIWN YTHKIGLKLP KDLPSEEKTV YRDLKKSKQE VGDGVLEFVI
YQSGVDLGLE FTLRGRAFRV HQGVGPWKIL FKEQVCNVYF QVDGEYYLMS YPDSLSIEHY
KKINVLKNMG HAKKMQITMW ANRIKLTVGY YRKGVTLNRI MYAIRSIHSE VEKFEKMSRN
LIQCIEKYKK EKQICISSYK NYKQEIKECA RSLFTDDILA SLKKKDFKIL LTYSILLSRR
VPLKREALKM VVLSYVQLLN TEQKKEGRSQ VTNQHNDVDT SLLLTLKYLL HLNVDHDKVI
YNYIYSELNN LIDEYTLEEL VETVKLISSF KDKKWINQKV FSRCINEIVK RSNQMEEDTS
NYLVTIIKSC SRLNCEIADI HMLLERLRDN YQKKEKKNLH TVIKVLYNLF LCNYQSYKNV
NQLIEFVKSE LMGIRKEEEY PTYKKYTYNN NVVLDTNHDL DGQASGNNSS NAAICNDNIR
NIHQIYFNTK ENSQMYAAPS APIASVSLYR LKFVDLIIRS DNFLYNTVYS PNSHFFDFVK
QLRVEGKDPR ETIFTKQATF FVKESGFKLA RKFVHIYPIV HLPEFQNTYV EFVHNRSINR
KMKDNPHKFH RHHLTYRIRN LKFLGWNPIL LYEHEWKKLR YLTTNIKKIY
//
