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Database: UniProt
Entry: A0A1I0GEQ5_9CLOT
LinkDB: A0A1I0GEQ5_9CLOT
Original site: A0A1I0GEQ5_9CLOT 
ID   A0A1I0GEQ5_9CLOT        Unreviewed;       296 AA.
AC   A0A1I0GEQ5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:SET69418.1};
GN   ORFNames=SAMN05660297_03178 {ECO:0000313|EMBL:SET69418.1};
OS   Natronincola peptidivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Natronincola.
OX   NCBI_TaxID=426128 {ECO:0000313|EMBL:SET69418.1, ECO:0000313|Proteomes:UP000199568};
RN   [1] {ECO:0000313|EMBL:SET69418.1, ECO:0000313|Proteomes:UP000199568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18979 {ECO:0000313|EMBL:SET69418.1,
RC   ECO:0000313|Proteomes:UP000199568};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC       {ECO:0000256|ARBA:ARBA00005983}.
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DR   EMBL; FOHU01000020; SET69418.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0GEQ5; -.
DR   STRING; 426128.SAMN05660297_03178; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000199568; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.200.40; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
DR   PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SET69418.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199568};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..132
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   296 AA;  33067 MW;  C407DF12C85AE13E CRC64;
     MEKIQVICNP NAGRQIVQKN IPKLVEVLNE DANREVDIYY TSKKFDARNK AEKSCYNQYD
     LIITIGGDGT VNEVINGMMQ SDKKPKLAIY PAGTVNDFGT YLKIPRNIEE FGKMLIRNNS
     TKVDVGVSGD RYFLNVAAAG LLPEVAHKVS SEAKTVLGKF AYYIEGIKEF SKQLFKPMRV
     KLYINGKEEE KEILFFILAN SPSVGGFSYL VPEARIDDGY LDLLMVEYSQ LKDVAGMFIK
     ALTGNHANHP ALKYLQVQEI SILTDNRIDL DLDGELGGSL PASFKVEKQA LEIIIP
//
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