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Database: UniProt
Entry: A0A0D0S495_9FIRM
LinkDB: A0A0D0S495_9FIRM
Original site: A0A0D0S495_9FIRM 
ID   A0A0D0S495_9FIRM        Unreviewed;       300 AA.
AC   A0A0D0S495;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Transcription regulator (Contains diacylglycerol kinase catalytic domain) {ECO:0000313|EMBL:KIR01167.1};
GN   ORFNames=P261_02877 {ECO:0000313|EMBL:KIR01167.1};
OS   Lachnospiraceae bacterium TWA4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR01167.1, ECO:0000313|Proteomes:UP000032079};
RN   [1] {ECO:0000313|EMBL:KIR01167.1, ECO:0000313|Proteomes:UP000032079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TWA4 {ECO:0000313|EMBL:KIR01167.1,
RC   ECO:0000313|Proteomes:UP000032079};
RX   PubMed=25495654;
RA   Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J.,
RA   Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.;
RT   "Investigation of a new acetogen isolated from an enrichment of the tammar
RT   wallaby forestomach.";
RL   BMC Microbiol. 14:314-314(2014).
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:KIR01167.1}.
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DR   EMBL; JPZU01000004; KIR01167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0S495; -.
DR   STRING; 1392836.P261_02877; -.
DR   PATRIC; fig|1392836.3.peg.3261; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000032079; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   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   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:KIR01167.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032079};
KW   Transferase {ECO:0000313|EMBL:KIR01167.1}.
FT   DOMAIN          1..134
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   300 AA;  33290 MW;  6393B8BFAC9BEACB CRC64;
     MSNKKMLFIF NPYSGKGQIK NNLVSILDTF IKAKYQINVH VTQEKGEATR IVRERAQDVD
     YVVCSGGDGT LHEVVNGVMS LPSEERPSIG YIPTGTTNDY GKSLKIPKDM KKAALMMAKC
     PSYLTDIGQF NDQYFTYVAG FGIFTAVSYT TPQDAKNMLG HPAYIIEGMK SLADIEPCHV
     KVISDEYSEE GDYLIGLVTN SISVSGSKLV PGKGAILDDG IFEVMLVKNP ENPLAMPQVL
     MEFLQDNPEN NSYVIRFKTS HIKFEVDKKI DWVLDGEFGG HLAEVDIQVK QKALAITRKN
//
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