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Database: UniProt
Entry: A0A1L8QNG3_9ENTE
LinkDB: A0A1L8QNG3_9ENTE
Original site: A0A1L8QNG3_9ENTE 
ID   A0A1L8QNG3_9ENTE        Unreviewed;       338 AA.
AC   A0A1L8QNG3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Lipid kinase {ECO:0000313|EMBL:OJG09064.1};
GN   ORFNames=RU93_GL001226 {ECO:0000313|EMBL:OJG09064.1};
OS   Enterococcus aquimarinus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=328396 {ECO:0000313|EMBL:OJG09064.1, ECO:0000313|Proteomes:UP000182149};
RN   [1] {ECO:0000313|EMBL:OJG09064.1, ECO:0000313|Proteomes:UP000182149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17690 {ECO:0000313|EMBL:OJG09064.1,
RC   ECO:0000313|Proteomes:UP000182149};
RA   Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT   "Draft genome sequences of 29 type strains of Enterococci.";
RL   Submitted (DEC-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJG09064.1}.
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DR   EMBL; JXKD01000021; OJG09064.1; -; Genomic_DNA.
DR   RefSeq; WP_071875666.1; NZ_JXKD01000021.1.
DR   AlphaFoldDB; A0A1L8QNG3; -.
DR   STRING; 328396.RU93_GL001226; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000182149; 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:SF115; DIACYLGLYCEROL KINASE; 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:OJG09064.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182149};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..133
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   338 AA;  37206 MW;  16FA75C6252C9B9E CRC64;
     MKKARVIYNP VAGKELMKKN LADILDVLEQ AGFEASAFAT TPEENSAKNE ARRVAEAGYD
     LVVAAGGDGT INEVVNGIAP LEKRPKMAII PGGTTNDYAR ALKIPRDNVR EAAKVVLKNQ
     TIKMDIGKAA DSYFINIAAG GHLTELTYEV PTELKSIFGY LAYLAKGAEL LPRIKPIPMH
     LKYDDGVYDG NASMFFLGLT NSVGGFEQIV PDAKLDDGKF SLIIVKTANV FEILHLVGLL
     INGGKHVNDR RIIYTKTSKL EVNLPDPNKR LMINLDGEYG GDAPMTFENF HNHIEFYGDL
     DAIPNQAVIG NAYEEVSKEF LEEVERLQES EFESPIEE
//
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