ID B9XF95_PEDPL Unreviewed; 300 AA.
AC B9XF95;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Diacylglycerol kinase catalytic region {ECO:0000313|EMBL:EEF61593.1};
GN ORFNames=Cflav_PD4272 {ECO:0000313|EMBL:EEF61593.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF61593.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF61593.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF61593.1,
RC ECO:0000313|Proteomes:UP000003688};
RX PubMed=21460084; DOI=10.1128/JB.00299-11;
RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT Verrucomicrobial isolate from pasture soil.";
RL J. Bacteriol. 193:2900-2901(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EEF61593.1}.
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DR EMBL; ABOX02000009; EEF61593.1; -; Genomic_DNA.
DR RefSeq; WP_007414485.1; NZ_ABOX02000009.1.
DR AlphaFoldDB; B9XF95; -.
DR STRING; 320771.Cflav_PD4272; -.
DR OrthoDB; 9786026at2; -.
DR Proteomes; UP000003688; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEF61593.1};
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:UP000003688};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..129
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 300 AA; 31636 MW; 7E664AC20A51BD90 CRC64;
MRTCVIFNPT AKGDKARRFR RNLDRIGAEC TLKQTTHAGA ARTLAAEAVQ EGFNIIVAAG
GDGTVNEVLN GIGDAPDGFK RACLGVFPLG TVNVFAKELG LPTEISQAWE IIKAGQETTI
DLPAVKFAGA GGASESRYFA QLAGAGLDAR AIELVDWQLK KKLGPLAYVW AGMMALRGKP
AQITVTNGTS SATGALVLVG NGRFYGGRYR VFPEADLQDG QLEVVVFPRA NWLTLARCSG
MFLAGQALPA SVAKSFKAHT LTLTSTSPTP LEVDGDNIGH LPAVMSIQRQ ALRVVVPGKG
//
