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Database: UniProt
Entry: A0A3B3SQX7_9TELE
LinkDB: A0A3B3SQX7_9TELE
Original site: A0A3B3SQX7_9TELE 
ID   A0A3B3SQX7_9TELE        Unreviewed;      1004 AA.
AC   A0A3B3SQX7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
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|Ensembl:ENSPKIP00000032748.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000032748.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000032748.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B3SQX7; -.
DR   Ensembl; ENSPKIT00000013621.1; ENSPKIP00000032748.1; ENSPKIG00000012653.1.
DR   GeneTree; ENSGT00940000156152; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000261540; 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: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; 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; PF00130; C1_1; 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|RuleBase:RU361128};
KW   Kinase {ECO:0000256|RuleBase:RU361128};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          307..441
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REPEAT          933..965
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          267..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          777..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..285
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1004 AA;  112603 MW;  3BC378569776D27A CRC64;
     MEQQQQQDAG ACFSQVPLPA TEELISSTTS SSSSTSDLPS SLPVEGELPV VAHHHTTKTF
     TGLRLFGRRK AIAKAGLQHL NAQPCASTVL RGDREHEIRS TVDWSENAVY GEHIWFETNV
     SGDFCYVGEQ HCIARTMQKS VPRKKCAACK IVVHTICIEQ LEKINFRCKP SFRESGSRNI
     REPTVVRHHW VHRRRQEGKC KQCGKGFQQK FAFHSKEIVA ISCSWCKQAY HNKVTCFMLQ
     QIEETCSLGA HAAVIVPPTW IIHVRRPQSS LKSSKKKKRT SFKRKSSKKG AEETRWKPFI
     VRPIPSQLMK PLLVFVNPKS GGNQGAKIIQ SFMWYLNPRQ VFDLSQGGPK DGLELYRRVH
     NLRILACGGD GTVGWILSTL DQLQLNPQPA VAVLPLGTGN DLARTLNWGG GYTDEPVSKI
     LSHVEDGNIV QLDRWNLIVE PNLEASQEEK DEQQTDKLPL DVFNNYFSLG FDAHVTLEFH
     ESREANPEKF NSRFRNKMFY AGTAFSDFLM GSSKDLAKHI KVVCDGTDLT SKVQELKLQC
     LLFLNIPRYC AGTMPWGNPS EHHDFEPQRH DDGCIEVIGF TMTSLATLQV GGHGERLNQC
     REVTLTTYKP IPMQVDGEPC KLAPSIIHIS LRNQANMVQK TKRRTSIPLL NDQQPIPERL
     RIRVNRISMH DYEALHYDKE KLKEASIPLG LIVIPGDSDL ETCRLHIERL QEEGDGTKLK
     TLSSQKLSPK WCFLDSTTAD RFYRIDRAQE HLNYVTEISQ DELFILDPEL VITETVGTSP
     GMPDLVDSSA EYPGPTRQFA FPSSSSPPAS PLPMILELQK ATQRKRISSD SAVAEAPTHG
     DPPRSPVSSP CRSEGTAICN TDKVSAEILF ECVKSKDHRM LKELHKLGAD LSVQDSSGCT
     LLHHAATAGS KEIVKYIIDN ASSDILDVTE KESGETVLHK AAAMRQRTIC HYLVEAGASL
     MKTDLQGDTP KHRAEKAKDP ELAAYLENRQ HYQMIQREDQ ETAV
//
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