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Database: UniProt
Entry: A0A3Q0GWD0_ALLSI
LinkDB: A0A3Q0GWD0_ALLSI
Original site: A0A3Q0GWD0_ALLSI 
ID   A0A3Q0GWD0_ALLSI        Unreviewed;      1163 AA.
AC   A0A3Q0GWD0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, 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   Name=DGKZ {ECO:0000313|RefSeq:XP_025063747.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025063747.1};
RN   [1] {ECO:0000313|RefSeq:XP_025063747.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00023371};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC         Evidence={ECO:0000256|ARBA:ARBA00023371};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC         + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023400};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC         Evidence={ECO:0000256|ARBA:ARBA00023400};
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   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00005175}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR   RefSeq; XP_025063747.1; XM_025207962.1.
DR   AlphaFoldDB; A0A3Q0GWD0; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000189705; Unplaced.
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:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
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; cd20849; C1_DGKzeta_rpt1; 1.
DR   CDD; cd20895; C1_DGKzeta_rpt2; 1.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR047485; C1_DGKzeta_rpt1.
DR   InterPro; IPR047484; C1_DGKzeta_rpt2.
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:SF43; DIACYLGLYCEROL KINASE ZETA; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          493..627
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REPEAT          1056..1079
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..503
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..1016
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1163 AA;  130138 MW;  5AA9C01FB377D1DF CRC64;
     METFFKRHFR KKGCSRSRRA SMAVPTGKVR RRSLVGQPSA SLAQHRRRSS TPLQGLSLCL
     GSPRKGRSST RRRSSTTPPC VSPRFSVQKK RGAQMRTIDT HLMGPSMLLA NLIQTREEEE
     GRRSPYEEGS GSESPQEGPE EEAYWEETVT SGSEEAEQDR HEQQALLPWQ TWPPVLRPLS
     VGHLLRAPRY LRRNSSRLLP ADVVYSKAAY GLYGSYRRLS QPRRASEVLT VGMLLPPDRA
     QLATKRQRAL SKGMPPALAA PHECLGAEPA YGPCTGASRE SWSPLLLKAI AKSGLQHMVA
     QPSPALALRS DPERQIRSTV DWSETAVYGE HIWFETNVSG DFCYVGEQNC VAKMLQKPLS
     RRKCAACKIV VHTPCIEQLE KINFRCKPSF RESGSRNIRE PAIVRHHWVH RRRQEGKCRQ
     CGKGFQQKFA FHSKEIVAIS CSWCKQAYHS KVSCFMLQHI EEPCSLGAHA AVVVPPTWIL
     RVRRPQNPLK SSKKKKRASF KRKSSKKGPE GAKIIQSFMW YLNPRQVFDL SQGGPKEALE
     MYRKVHNLRI LACGGDGTVG WILSILDQLR LNPPPPVAIL PLGTGNDLAR TLNWGGGYTD
     EPLSKILSHV EDGNIVQLDR WNLHVEPNTE ASPEEKDETA TDKLPLDVFN NYFSLGFDAR
     VTLEFHESRE ANPEKFNSRF RNKMFYAGTA FSDFLTGSSK DLAKHVKLVC DGADLTSKIQ
     DLKPQCLVFL NIPRYCAGTM PWGNPGEHHD FEPQRHDDGC IEVIGFTMTS LAALQVGRHG
     ERLCQCRQVL LTTSKAIPMQ VDGEPCKLAP SSIHISLRNQ ANMVQKTKRR NSMPLLNDQQ
     PVPERLRIRV SRISMHDYEA LHYDKEKLKE ASVPLGIIVV PGDSDLEMCR TQIEKLQEDF
     PSCPSALQRL LLQEGDGAKP KALSSQKLSP KWCFLDATTA DRFYRIDRAQ EHLNYVTEIS
     QDELFVLDPE LVITQTVGTS PAMPDLVDTS STPTGHHFAF PSSSSSPPSS PAPSSEAGVG
     PTHKDNPLIE AAKSGDFSKF QELHRAGGDL MVRDSSGQTV LHLAVKSGSK DIVKYIIENA
     PSEILDATEE KNSETSLHQA AALRQRTICH YIVEAGASLM KTDLQGDTPK HRAEKANDPD
     LAAYLENRQH YQMIQREDQE TAV
//
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