ID A0A2H5PUE5_CITUN Unreviewed; 732 AA.
AC A0A2H5PUE5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=CUMW_168120 {ECO:0000313|EMBL:GAY55962.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY55962.1, ECO:0000313|Proteomes:UP000236630};
RN [1] {ECO:0000313|EMBL:GAY55962.1, ECO:0000313|Proteomes:UP000236630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
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:GAY55962.1}.
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DR EMBL; BDQV01000128; GAY55962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5PUE5; -.
DR STRING; 55188.A0A2H5PUE5; -.
DR Proteomes; UP000236630; 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:SF54; DIACYLGLYCEROL KINASE THETA; 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|ARBA:ARBA00023136, 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:UP000236630};
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 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..140
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 152..215
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 361..500
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 263..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 81167 MW; 4454487F059FD2E1 CRC64;
MEHDREMNLW LPGWNSGSQA EMTESRLFIL SCFIAALIGI LTIAYTAFQW RRNINLGWMK
AIARSKKNPK TRHKVPLAPH TWVLESVSRG KNLNCCVCLK SMSPSQTLGP MVASDSFIHR
CSICGAAAHL SCSLSAHKDC KCVSMIGFDH VIHQWSVRWT EITDQPSEAS FCSYCEEPCS
GSFLGGSPIW CCLWCQRLVH VDCHNNMSNE TGDICDLGPF RRLILSPLYV KELNHTLAGG
ILSSITHGAN EIASQVRASI RSQSKKYKHG NEPSVDPVDS GSTGDTSSES MADAHKTVHS
SNRVEENCNG GTNVGDHYQD GELDRKIESK PSFKRSGSIN QKDESQILQL KQKYELIDMP
PDARPLLVFI NKKSGAQRGD SLRQRLNLLL NPVQVVELSS TQGPEVGLFL FRKVPHFRVL
VCGGDGTVGW VLNAIDKQNF VSPPPVAILP AGTGNDLARV LFWGGGLSSV ERNGGLCTML
QHIEHAAVTI LDRWKVAILN QQGKLLEPPK FLNNYLGVGC DAKVALDIHN LREENPEKFY
NQFMNKVLYA REGAKSIMDR TFEDFPWQVR VVVDGTEIEV PEDAEGVLVA NIGSYMGGVD
LWQNEDENYD NFDPQSMHDK VLEVVSISGT WHLGKLQVGL SRARRLAQGQ SIRIQLFAPL
PVQIDGEPWF QQPCTLAISH HGQAFMLKRA AEEPLGHAAA IITDVLESAE TNRVINASQK
RALLQEMALR LS
//
