ID A0A314ZMA8_PRUYE Unreviewed; 709 AA.
AC A0A314ZMA8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=Pyn_28709 {ECO:0000313|EMBL:PQQ19830.1};
OS Prunus yedoensis var. nudiflora.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=2094558 {ECO:0000313|EMBL:PQQ19830.1, ECO:0000313|Proteomes:UP000250321};
RN [1] {ECO:0000313|EMBL:PQQ19830.1, ECO:0000313|Proteomes:UP000250321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jeju island {ECO:0000313|Proteomes:UP000250321};
RC TISSUE=Leaf {ECO:0000313|EMBL:PQQ19830.1};
RA Baek S., Kim J.-H., Choi K., Kim G.-B., Cho A., Jang H., Shin C.-H.,
RA Yu H.-J., Mun J.-H.;
RT "Draft genome of wild Prunus yedoensis var. nudiflora.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:PQQ19830.1}.
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DR EMBL; PJQY01000055; PQQ19830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A314ZMA8; -.
DR STRING; 2094558.A0A314ZMA8; -.
DR Proteomes; UP000250321; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; 2.60.200.40; -; 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:SF104; DIACYLGLYCEROL KINASE 2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
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|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW Reference proteome {ECO:0000313|Proteomes:UP000250321};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..134
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 146..205
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 338..477
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 709 AA; 79682 MW; 55C1FC3A5FBAF080 CRC64;
MMVDLGISLA KVVTSLDGYG PFLLGWLVTG SFGLLAIIFA FLKWQRRTSL NWVKAAAREK
KKVWKKLKVP LSHHTWMEDM TNGEQPSTCC VCLTSLVFLH NLGTKASYRT PVHRCSVCGV
AAHFYCSQYA VRDCKCVAQA GFTHVRHHWS ERWVNMHDNP EISVFCFYCD EPCGVPLLDA
SPTWHCLWCQ RLIHVRCHNK MAKECGDACD FGTLSRIIIS PLCVKEVGHY NGGGMLSSYT
DEMITSPVRR QYRRKRRHCK HGNGQSANGN LATDAPVECV FNGFTRMKKS RSEKSFDYLN
KDDKALIVKG NHNGFMQRQG GTVTYGQIKK YKLVDLPHDA RPLLVFINAR SGGQNGASLR
RRLNMLLNPV QVFELSSSQG PEVGLELFNH VQYFRVLVCG GDGTVAWVLD AIERHKFESP
PPVAILPLGT GNDLSRVLQW GRGFSTVDGQ GGLTMLLHEI NHAAVTMLDR WKVNIKSEAD
PNKVQSKFMM NYLGIGCDAK VAYEFHVTRE INPEKFSSQF VNKLRYAKEG ARDIMDRTCA
DLPWQVWLEV DGEDIDIPKD SEGLIVLNIG SYMGGVNLWQ NDIEHDDEFS LQSMHDKMLE
VVCICGAWHL GKLQVGLSHA RRLAQGKVIR IHASSPFPVQ IDGEPFIQQP GCLEITHHGQ
MFMLRRASEE PRGHAAAIMA EVLLDAECKG IINASQKKIL LQQMALQLN
//
