The domain within your query sequence starts at position 673 and ends at position 702; the E-value for the ANK domain shown below is 8.39e-3.



ankyrin repeats
SMART accession number:SM00248
Description: Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Interpro abstract (IPR002110):

The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers [(PUBMED:8108379)]. The repeat has been found in proteins of diverse function such as transcriptional initiators, cell-cycle regulators, cytoskeletal, ion transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it.

The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [(PUBMED:8875926), (PUBMED:9353127), (PUBMED:9461436), (PUBMED:9865693)]. Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90o angle. The repeats stack together to form an L-shaped structure [(PUBMED:8875926), (PUBMED:12461176)].

GO function:protein binding (GO:0005515)
Family alignment:
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There are 1471345 ANK domains in 265757 proteins in SMART's nrdb database.

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