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Database: UniProt
Entry: A0A1D6K5X7_MAIZE
LinkDB: A0A1D6K5X7_MAIZE
Original site: A0A1D6K5X7_MAIZE 
ID   A0A1D6K5X7_MAIZE        Unreviewed;       555 AA.
AC   A0A1D6K5X7;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=diacylglycerol kinase (ATP) {ECO:0000256|ARBA:ARBA00012133};
DE            EC=2.7.1.107 {ECO:0000256|ARBA:ARBA00012133};
GN   ORFNames=ZEAMMB73_Zm00001d029550 {ECO:0000313|EMBL:ONL98968.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONL98968.1};
RN   [1] {ECO:0000313|EMBL:ONL98968.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONL98968.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000256|ARBA:ARBA00009280}.
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DR   EMBL; CM007647; ONL98968.1; -; Genomic_DNA.
DR   EMBL; CM007647; ONL98975.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6K5X7; -.
DR   ExpressionAtlas; A0A1D6K5X7; baseline and differential.
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   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; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ONL98968.1};
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   Plant defense {ECO:0000256|ARBA:ARBA00022821};
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        25..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..141
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          153..216
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          345..505
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          255..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  62317 MW;  F055A7E70240974F CRC64;
     MVWLQDQLEM HKFHWYSRAP TPSEFWIPLA AWFTVGLVGL WTFFHFFSVW RRKISLSWMK
     IIARSKRKNF ERNHEVPTAE HVWNTESLIR AKGMMCCVCL ESISPAQPLG QMMTSENMVH
     RCNVCGAAAH IICSSNSQKD CKCISMFGFK HVVHQWTVLW TDIADQSEEG QYCSYCEELC
     SESFLGGPPI YCCMWCQRLV HADCQSAMAT ETGEICDLGP FKRLILSPLF VRAISKPGSI
     LSSITHGANE FATTVRGRLN RTKKEKHQNR FSSDSNDDSS SDTTLNSNQR AGELKTIGDS
     AQRSPENEHD SSESDGRELI SESRRLGNDE TGEVKLKYAL SELPADSRPL LIFINKKSGA
     QRGDLLKHKL HFLLNPVQVM ILLTQNFTLS RVTSQLGNMV FELSSSQGPE TGLFLFRKVP
     HFRILVCGGD GTVGWVLDAI DKQNYESPPP IAILPAGTGN DLSRVLSWGG GLGAVEKQGG
     LCTILHDIEH AAVTILDRWK VTVEDKKSKN VLLVKYMNNY LGIGCDAKVA LDIHNLREGN
     PEKFYSQVMF VLYPS
//
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