The domain within your query sequence starts at position 132 and ends at position 274; the E-value for the DAGK_cat domain shown below is 1.1e-31.
HLLVFINPFGGKGQGKRIYEKTVAPLFTLASITTEIIITEHANQAKETLYEINTDSYDGI VCVGGDGMFSEVLHGVIGRTQQSAGIDPNHPRAVLVPSTLRIGIIPAGSTDCVCYSTVGT NDAETSALHIIIGDSLAIDVSSV
DAGK_cat |
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PFAM accession number: | PF00781 |
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Interpro abstract (IPR001206): | The DAG-kinase catalytic domain or DAGKc domain is present in mammalian lipid kinases, such as diacylglycerol (DAG), ceramide and sphingosine kinases, as well as in related bacterial proteins [ (PUBMED:8626538) (PUBMED:17351295) ]. Eukaryotic DAG-kinase ( EC 2.7.1.107 ) catalyses the phosphorylation of DAG to phosphatidic acid, thus modulating the balance between the two signaling lipids. At least ten different isoforms have been identified in mammals, which form 5 groups characterised by different functional domains, such as the calcium-binding EF hand PH SAM DAG/PE-binding C1 domain and ankyrin repeats [ (PUBMED:17512245) ]. In bacteria, an integral membrane DAG kinase forms a homotrimeric protein that lacks the DAGKc domain. In contrast, the bacterial yegS protein is a soluble cytosolic protein that contains the DAGKc domain in the N-terminal part. YegS is a lipid kinase with two structural domains, wherein the active site is located in the interdomain cleft, C-terminal to the DAGKc domain which forms an alpha/beta fold [ (PUBMED:17351295) ]. The tertiary structure resembles that of NAD kinases and contains a metal-binding site in the C-terminal region [ (PUBMED:17351295) (PUBMED:19112175) ]. This domain is usually associated with an accessory domain (see IPR000756 ). |
GO function: | kinase activity (GO:0016301) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry DAGK_cat