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Database: UniProt
Entry: A0A3B3YC55_9TELE
LinkDB: A0A3B3YC55_9TELE
Original site: A0A3B3YC55_9TELE 
ID   A0A3B3YC55_9TELE        Unreviewed;      1073 AA.
AC   A0A3B3YC55;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
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};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000024931.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000024931.1}
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=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_014857643.1; XM_015002157.1.
DR   AlphaFoldDB; A0A3B3YC55; -.
DR   STRING; 48701.ENSPMEP00000024931; -.
DR   Ensembl; ENSPMET00000006359.1; ENSPMEP00000024931.1; ENSPMEG00000007748.1.
DR   GeneID; 106926941; -.
DR   KEGG; pmei:106926941; -.
DR   OrthoDB; 4642163at2759; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000261480; 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: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; cd13274; PH_DGK_type2; 1.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF33; DIACYLGLYCEROL KINASE KAPPA; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
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   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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          50..143
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          160..210
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          232..283
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          313..448
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          556..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1020..1073
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1035..1050
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1073 AA;  119378 MW;  5972AC7B762A6A8D CRC64;
     MLGFSRLSGC CAALLLRRRL GDDVRLRQDY CSLASRVCEE PQESVLEDEK SVKEGILLKQ
     TSSFQRWKRR YFKLRGRTLY YAKDCKSLIF DEVDLSDASV AETSTKNINN SFTVITPFRK
     LMLCAESRKE MEDWITALKS VQKWETYEAS QFNMEHFSGM HNWYACSHAR PTFCNVCKEA
     LPGVTSHGLS CEVCKFKAHK RCAVRSTNNC KWTTLASIGN EIIEDEDGVS MPHQWLEGNL
     PVSAKCVVCD RNCGSVRRLQ DWRCLWCKAI VHNSCKEQMG KVCPLGQCRV SIIPPTALNS
     IDSDGFWKAT SGSCASPLLV LVNSKSGDNQ GVKFLRKFKQ LLNPAQVFDL MNGGPELGLR
     LFQKFVTFRI LVCGGDGSVG WGLSELDKHN LHKQCQLGVL PLGTGNDLAR VLGWGGLCDD
     DAQLLQILEK LERATTKMLD RWSVMTYEVP PTNKQTPTVK EDDSHEAPLQ VHITQYADSV
     ACHLAKILDS DKHSDVISSA KFLCGTVNDF VAEVGKAYER ATENKEEADA MAKKCALLNE
     KLDSLVKALS EEAEAQVVPA GSAPSQESGG SSPGESGGES GSEGKTYRSK EQLMLRANSL
     KKALRQIIEQ AEKVVDEQNR HTQVQRMPSS SSITRENSEE LKDADTRGLS PTSPIVLEKT
     ESLNAVTFNE DTVQCTEKCV MNNYFGIGLD AKISLEFNNK RDEHPKKCSS RTKNMMWYGV
     LGTKELVQKT YKNLEQRVQL ECDGVAMSLP SLQGLAVLNI PSYAGGINFW GGTKEDNNFG
     APSFDDKKLE VVAVFGSMQM AMSRVINLQH HRIAQCRQVK ITILGDEGVP VQVDGEAWIQ
     PPGIVKIVHK NRAQMLTRDR AFESTLKSWE DKRKIDSYRT ARPRLNSQQS MEYLTEEECA
     QVQQLGIVAD TLINKIREAA KTHKLVEQEL AHAVNATALV LTEAKVSSNE CLSRSTAVEI
     VNSSKVLQAE TSMLLDGKLL SDFPEEEELR LTLNNLSAEL LKLDDIHWIC PLMQCSEEDS
     VRSGSKGTSS MKLKIIPKTK KEKEKLHKQK SNSSLSGTWD LKSGAAEADS SVN
//
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