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ADF Domain
Class:Cytoskeletal modulation

Domain binding and function:
 structure The Actin-Depolymerizing Factor (ADF) homology domain or ADF domain is a 130-170 amino acid domain, first identified in the ADF family of proteins, that is associated with proteins involved in F-actin severing. The domain functions as an actin-binding module present in an extensive family of proteins, including ADF/Cofilin, the Twinfilins and Drebrin/Adp1. This evolutionarily primitive domain pre-dates the divergence of fungi and animals and is found in all eukaryotic organisms. The ADF-containing proteins ADF, Cofilin, Depactin and Actophorin bind to monomeric and filamentous actin and act to sever Actin filaments. This creates more plus (barbed) and minus (pointed) ends allowing faster Actin turnover and results in the observation that these proteins both rapidly depolymerize filamentous Actin in vitro, as well as increase the rate of F-actin polymerization. Certain ADF-containing proteins appear to have developed more specialized functions as Drebrin/Adp1 class proteins bind only filamentous actin, while Twinfilins bind only monomeric Actin.
Examples of Proteins: 
ADF domain protein
Binding partner
ADF/Cofilin Filamentous and monomeric actin
Drebrin Filamentous actin
Twinfilins Monomeric actin

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