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Database: UniProt
Entry: R2QVG5_9ENTE
LinkDB: R2QVG5_9ENTE
Original site: R2QVG5_9ENTE 
ID   R2QVG5_9ENTE            Unreviewed;       329 AA.
AC   R2QVG5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=YegS//BmrU family lipid kinase {ECO:0000313|EMBL:EOH75470.1};
GN   ORFNames=UAK_03303 {ECO:0000313|EMBL:EOH75470.1};
OS   Enterococcus raffinosus ATCC 49464.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1158602 {ECO:0000313|EMBL:EOH75470.1, ECO:0000313|Proteomes:UP000013877};
RN   [1] {ECO:0000313|EMBL:EOH75470.1, ECO:0000313|Proteomes:UP000013877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49464 {ECO:0000313|EMBL:EOH75470.1,
RC   ECO:0000313|Proteomes:UP000013877};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus raffinosus ATCC_49464.";
RL   Submitted (FEB-2013) 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:EOH75470.1}.
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DR   EMBL; AJAL01000018; EOH75470.1; -; Genomic_DNA.
DR   RefSeq; WP_010746482.1; NZ_KB946259.1.
DR   AlphaFoldDB; R2QVG5; -.
DR   PATRIC; fig|1158602.3.peg.3305; -.
DR   eggNOG; COG1597; Bacteria.
DR   HOGENOM; CLU_045532_0_2_9; -.
DR   OrthoDB; 9786026at2; -.
DR   Proteomes; UP000013877; 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: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:SF54; SPHINGOID LONG-CHAIN BASES KINASE 2, MITOCHONDRIAL; 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:EOH75470.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..147
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   329 AA;  36905 MW;  9F67A9445CB9BFBB CRC64;
     MNFHYHILIN PAAGSGNAAK TAKKIIQLLD DGDYTYTPYY TEKPGDEREI VERLVELLSP
     WSKDCEKEHI DHSFHLLVVI GGDGTLHQVV NQFYAMDIQR PVSYIPAGSG NDFARGIGLS
     RDPEKAFEQI TSALQPQPIN VFHYEEKIRE EQGIILNNVG IGLDALIVAT TNASTSKKVL
     NKYHLGSASY ALYLVKAIFT QKTFPILVEL NGQSLSFQRT FLCTTTNIPY FGGGVAIAPM
     ADPKKDAIDL VVVEKPDLPA ILRFLLQLLR KKHTTNKHYQ HFTSSKIRIV SVVPQHGQAD
     GEDMGERSFD MNFSTATQYI WYADKRTEK
//
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