The domain within your query sequence starts at position 152 and ends at position 293; the E-value for the DAGK_cat domain shown below is 2.6e-27.



PFAM accession number:PF00781
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 ) 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