ID A0A1Y1JCY4_PLAGO Unreviewed; 1455 AA.
AC A0A1Y1JCY4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=diacylglycerol kinase (ATP) {ECO:0000256|ARBA:ARBA00012133};
DE EC=2.7.1.107 {ECO:0000256|ARBA:ARBA00012133};
GN ORFNames=PGO_072840 {ECO:0000313|EMBL:GAW80369.1};
OS Plasmodium gonderi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=77519 {ECO:0000313|EMBL:GAW80369.1, ECO:0000313|Proteomes:UP000195521};
RN [1] {ECO:0000313|Proteomes:UP000195521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30045 {ECO:0000313|Proteomes:UP000195521};
RA Arisue N., Honma H., Kawai S., Tougan T., Tanabe K., Horii T.;
RT "Plasmodium gonderi genome.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280}.
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:GAW80369.1}.
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DR EMBL; BDQF01000008; GAW80369.1; -; Genomic_DNA.
DR EnsemblProtists; GAW80369; GAW80369; PGO_072840.
DR OMA; IHKLHFT; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000195521; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd00029; C1; 1.
DR CDD; cd20805; C1_DGK_rpt2; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
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 InterPro; IPR002219; PE/DAG-bd.
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; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 2.
DR PROSITE; PS50146; DAGK; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GAW80369.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000195521};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 26..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..175
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 404..483
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT DOMAIN 1017..1095
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 314..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1455 AA; 168521 MW; C035BC17D8AFB272 CRC64;
MEDFAYVDKN VYINILLTIL NKCKEYLLGI GILKLTLCLC IILISIIFAK RKNKKKKKIS
IYIQLNNVRK NNNKDEKLID NEKCSFPNEE AKITEPDFSK LCEHTDGEKG NNEFYYISYS
PHIFDLKSIS RTELCNVCNE SIYSFIFYKK DIFECVVCRN KCHIECAPNS NLMSCKTSVF
FKNKHKFIKI RNCLWNNKCD ICNKKFSYFS FPPFVKQYIY NCIWCNKYFH VHCIAKISDK
RKNTRGKNQV KDALCTYGNR KYILYPYEVS IKENILIDFL THAYHLVKES EITNDEVLLS
YSCNKFNVTI KDDGEDEDTS NHCEKKPNEG VMKEKEKEKG GHCSTTLKNT DEVLYLDYVN
DFHKFNKIRK FKNANKTKKH VIPVHANFLL NFFPIHLPIY EIKSSDKFLL IFVNVKSGGQ
AGKKLYQQLL MYFNPLQIIS IKNEKNVLSA LNMYKEMLYL NKVILLLCGG DGTISIFVDT
LLKFFSKQVS FAIEQGKMKK KNNKLCSNEN KSEQYYSYTK STFLNKTIMN ITAKLKHNKD
AFRKKWTNNI TSQSKKPITF FLKKRSEKNT FNTDNDSGHI SEENAETYFE NDLCEAHMWG
ENNSENSKLK MSRRFTGSRR IDDPTTLCAS GKCVFSGVLG QLPDEIHHKD KSHAGRTYNG
IYHLDGNTDM NANINSRINS DENNLSGGGN MHNEMSSEMN SSGPGGTVPN DPDKRGTEAK
CTNGKYLYMH EKFKNFNKKK NGKHDTNDEK GEKIYANSEH VGEKGTYIEN GGEIGTYIGN
DREKGTNIGN GGEDCVKGGG DDKDGWKEST LKSFQNGNSM IEKYYNSNTM IHSNYTENNE
YLYSSSKGTE NDKMYYNILY HDYKEKVTSC SSMKTKINEN FTSYFNDANM TNQAYETNGT
TGEENTYTID NKQYNNVFNS NCSNNNSLVN DGSCNSDCRP PLCICNGEHL AHLEKVEQEN
LKGKGNRRNE EHLNLGQLDS YKSDENNIIY KIDNYYKIAY PKEKRNEKNY HNICEENDII
NNVITGEDKE MYNLKPTLQS YISNTPISIL PLGTGNDLSY SLGWGCGYNN DPLVYLNKVK
DCKNEYVDVW NMKAYDLDNN LILNNSFINY FDIGIISRLA LHFDNIRKKF PHFFNSRIGN
KILYGEVGFR DFCFNTYKYK LNKNIKLYCD GKKVKIDEDL ESVCLINVPY FLGGLKIWKE
DEQEKNYYSD VDRQKEEYKK KKRNKKGRKS LVEENKATNS SSNSSFLCHS TRDKVVHNEK
NHDGTISNNI NDKTTFYNSE KVTEEFLIHD TSKHSAEGEK VDLDPHSENS KNGNTSSQKH
PEEGEESSIE EKKKPSVHTN DNMFDCSNIY KSYRLDFYRQ KKNKQKYRKQ KMDDKVIEVI
GFRNMFHLLQ VQIGMSKAIK LCQGSEIKVK IDKTFIQNKN KIYFQYDGEP GFLNIHKLHF
THKCQCLFLS PKDPI
//
