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Database: UniProt
Entry: I3J9C8_ORENI
LinkDB: I3J9C8_ORENI
Original site: I3J9C8_ORENI 
ID   I3J9C8_ORENI            Unreviewed;       920 AA.
AC   I3J9C8;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   24-JAN-2024, entry version 65.
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=DGKQ {ECO:0000313|Ensembl:ENSONIP00000005468.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005468.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000005468.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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=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_003447693.1; XM_003447645.4.
DR   AlphaFoldDB; I3J9C8; -.
DR   STRING; 8128.ENSONIP00000046828; -.
DR   Ensembl; ENSONIT00000005472.2; ENSONIP00000005468.2; ENSONIG00000004338.2.
DR   GeneID; 100701920; -.
DR   KEGG; onl:100701920; -.
DR   CTD; 1609; -.
DR   eggNOG; KOG1169; Eukaryota.
DR   GeneTree; ENSGT00940000159492; -.
DR   HOGENOM; CLU_003770_0_0_1; -.
DR   OrthoDB; 4642163at2759; -.
DR   TreeFam; TF312817; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000005207; Linkage group LG2.
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:0048468; P:cell development; IEA:UniProt.
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; cd20803; C1_DGKtheta_typeV_rpt1; 1.
DR   CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1.
DR   CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1.
DR   CDD; cd17111; RA1_DAGK-theta; 1.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.30.60.20; -; 2.
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   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF34; DIACYLGLYCEROL KINASE THETA; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF00788; RA; 1.
DR   SMART; SM00109; C1; 3.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00314; RA; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          45..93
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          106..153
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          168..219
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          374..473
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          563..700
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..920
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   920 AA;  101884 MW;  9A0756BAB7641AF7 CRC64;
     MADSGRPRPA DPDAAESRTA SPLAGKKRAQ QSPGLRSKYQ SSAPGHCFKK VTLTKPTFCH
     SCSDFIWGII GFLCEVCNFM CHEKCLKTLR KVCSSMTPSL VQVPVAHCFG PAGQKKRFCC
     VCRKQTEGST ALRCEVCELH VHADCAIFTC ADCRSCHLDG ILEQDTFHHH WREGNLASAA
     RCEVCRRSCG SSDVLAGMRC EWCGITSHAA CYLAVPAECT LGRLRCMLLH PACVRLDSRN
     FSKMHCYRIA ESCSHELDNS DDGDLSAAAA PASKDGQPAA SESGKQNLKV FDGDDAVKRG
     FFRLVSITKN EEVVEAALRA FYLPDDPQDF ELHEIGGLQR LHSDDILNRN GGPDNRNSLK
     DGGDSWLLKA KPRVTEVIKV YNDWPRSGVA FISVSVSDSS TTSSVLAEVL SKLDRQEEDL
     SKFSLLEVCM SSKQVQRQTL TPQEKLLDKL REIRKVSLRQ MNQTRFYIVE NKNRAVRVEL
     LIGGLPPLLT TEKYTQLIEE HLAIKSHLVT ISNFYLNQGA VALQISCFAE AERIYMLAKD
     TSINNKTLTS LVIPGITHNT LGEDVCPLLV FVNPKSGGLK GRELLYGFRK LLNPHQVFDI
     MNGGPLAGLH TFREVPRFRV LVCGGDGTVG WVLGVLEAVR HKLTCREPPI GIIPLGTGND
     LARILRWGPG YSGEDPYHIL VSVYEADEVL MDRWTILLDA QDVSEDGKDN DFLEPPKIVQ
     MNNYFGLGID AELSLDFHLA REDEPDKFTS RFHNKGVYVK VGLQKISHTR SLHKELQLHV
     DGQEVPLPNI EGLIFLNIPS WGSGADLWGS EVDSRYEKPS IDDGLLEVVG VTGVVHMGQV
     QSGFRSGIRI AQGNYIRLTL RKPIPVQVDG EPWIQPPGHI IISAAGPKVR MLRKSKQKQK
     KSSANMRDGH SDSPSSRDGH
//
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