ID R5S389_9FIRM Unreviewed; 297 AA.
AC R5S389;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:CCZ45354.1};
GN ORFNames=BN483_00570 {ECO:0000313|EMBL:CCZ45354.1};
OS Firmicutes bacterium CAG:129.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263003 {ECO:0000313|EMBL:CCZ45354.1, ECO:0000313|Proteomes:UP000018410};
RN [1] {ECO:0000313|EMBL:CCZ45354.1, ECO:0000313|Proteomes:UP000018410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:129 {ECO:0000313|Proteomes:UP000018410};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCZ45354.1}.
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DR EMBL; CBAB010000005; CCZ45354.1; -; Genomic_DNA.
DR AlphaFoldDB; R5S389; -.
DR Proteomes; UP000018410; 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:CCZ45354.1};
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:UP000018410};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..133
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 297 AA; 32637 MW; 369C83D348D7888D CRC64;
MEKKLLFIVN PRAGKTKSRA PLFDAVSIFS KAGYLVRVAE TRRHGDATEL AERFGGDFDL
VVCHGGDGTL NETVNGIMRL PREKRPPLSY LPGGSTNDFA ASLSISSDPA LAAQSAMRLQ
PRDLDVGVFN EKNFVYVASF GAFTRTAYTV PQDIKNMFGH FAYLLEGVKD LETLCPYPMK
ITADGEVFEG EYLFGAVCNS TSIAGLMKLS PDAVDLCDGQ FELMLVPVPK TPLQLQRTIR
AIVYEEYETS NALIFRHVRH VTAESDGSIP WTLDGEYAPG VPKIEIGIED NGIQMMI
//
