ID U7UI59_9FIRM Unreviewed; 303 AA.
AC U7UI59;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Lipid kinase, YegS/Rv2252/BmrU family {ECO:0000313|EMBL:ERT59035.1};
DE EC=2.7.1.- {ECO:0000313|EMBL:ERT59035.1};
GN ORFNames=HMPREF1253_1971 {ECO:0000313|EMBL:ERT59035.1};
OS Peptoniphilus sp. BV3C26.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=1111134 {ECO:0000313|EMBL:ERT59035.1, ECO:0000313|Proteomes:UP000017105};
RN [1] {ECO:0000313|EMBL:ERT59035.1, ECO:0000313|Proteomes:UP000017105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3C26 {ECO:0000313|EMBL:ERT59035.1,
RC ECO:0000313|Proteomes:UP000017105};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-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:ERT59035.1}.
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DR EMBL; AWXB01000041; ERT59035.1; -; Genomic_DNA.
DR AlphaFoldDB; U7UI59; -.
DR STRING; 1111134.HMPREF1253_1971; -.
DR PATRIC; fig|1111134.3.peg.913; -.
DR eggNOG; COG1597; Bacteria.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000017105; 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:ERT59035.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000017105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ERT59035.1}.
FT DOMAIN 1..128
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 303 AA; 34801 MW; 1044897739712DBD CRC64;
MKYLFIYSTK AGKNDFNKFH REIKDFFIKK SLIENCQFVF TEDENHGRRA AKKFALENKE
GIVYACGGDG TLSEIANVLK NTNIALGLIP MGTANDFSKI FDYEKFTLDD LINPQIKKID
TIEINKTHTS INIASTGLDT RVLEYAREYA KKYKFLGKRI YDLATLKVLF NNRGQKIKMF
IDEKIIEGTY TLCAFCNGSY YGGGFNPAPN SILNDGKMEI VLAEFLKVPE IIRLIPKYKK
GQIFNEDKIK IFKAENVKIE LPEEINLNID GELLKDREFN LKLNKENLKF AILANLKNKN
QIK
//
