The domain within your query sequence starts at position 595 and ends at position 870; the E-value for the DDHD domain shown below is 3.75e-106.



SMART accession number:SM01127
Description: The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3) ((PUBMED:10022914)). This suggests that this region is involved in functionally important interactions in other members of this family.
Interpro abstract (IPR004177):

The Nir/rdgB (N-terminal domain-interacting receptor/Drosophila retinal degeneration B proteins) family has been identified in a variety of eukaryotic organisms, ranging from worms to mammals. Members of this family are implicated in regulation of lipid trafficking, metabolism, and signaling. The Nir/rdgB proteins contain a 180 amino-acids-long conserved region in the central part of the protein. This domain contains four conserved residues, DDHD, which may form a metal-binding site. This domain is named DDHD after these four residues. This pattern of conservation of metal-binding residues is often seen in phosphoesterase domains [ (PUBMED:15194420) ].

The DDHD domain is found in the central part of Nir/rdgB proteins, as well as the C-terminal part of the phosphatidic acid-preferring phospholipase A1. The DDHD domain function is not currently known but it may be implicated in phospholipid metabolism, membrane turnover, or intracellular trafficking [ (PUBMED:15194420) ].

GO function:metal ion binding (GO:0046872)
Family alignment:
View or

There are 5144 DDHD domains in 5140 proteins in SMART's nrdb database.

Click on the following links for more information.