The domain within your query sequence starts at position 180 and ends at position 319; the E-value for the DBB domain shown below is 8.55e-75.



Dof, BCAP, and BANK (DBB) motif
SMART accession number:SM01282
Description: The DBB domain is named from the Drosophila (Downstream of FGFR - Dof, also known as Heartbroken or Stumps) protein, the BANKS and BCAP, both signalling in B-cell pathway, proteins. This domain defines a minimal region required for mediating Dof dimerisation. Since this domain can interact both with itself and with a region in the C-terminal part of the molecule, it may mediate either intermolecular or intramolecular interactions PMID:12767830. Mutants lacking this domain disrupt FGFR signal transduction and fibroblast growth-factor signalling PMID:14993266.
Interpro abstract (IPR017893):

This entry represents the DBB domain.

The following proteins share a number of distinct parts, namely with ankyrin repeats a coiled coil, and a stretch of approximately 140 amino acid residues the development of the immune system in higher upstream of the ankyrin repeats, which has been called the Dof/BCAP/BANK (DBB) domain [(PUBMED:12767830), (PUBMED:14993266)]:

  • Drosophila Downstream-of-EGF receptor (Dof), a protein essential for the morphogenesis of both the mesoderm and the tracheae. It has been proposed to mediate the transmission of a signal from an activated receptor to other components of the cell, including the MAP kinase cascade.
  • Vertebrate BANK and BCAP proteins that function in B-cell signalling.

These proteins are involved in signalling; however, unlike Dof, BANK and BCAP are not implicated in FGF signalling but appear to have undergone rapid change during the course of evolution to acquire a novel function with vertebrates.

The DBB domain in both Dof and BCAP is required to mediate self-association in yeast cells, indicating that this domain may have a more general role in mediating protein-protein interactions [(PUBMED:12767830)].

Family alignment:
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There are 773 DBB domains in 773 proteins in SMART's nrdb database.

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