FLYWCH zinc finger


In molecular biology, the FLYWCH zinc finger is a zinc finger domain. It is found in a number of eukaryotic proteins. FLYWCH is a C2H2-type zinc finger characterised by five conserved hydrophobic residues, containing the conserved sequence motif:
 F/Y-X-L-X-F/Y-X-WXCXCXHXH
where X indicates any amino acid. This domain was first characterised in Drosophila modifier of mdg4 proteins, Mod, putative chromatin modulators involved in higher order chromatin domains. Mod proteins share a common N-terminal BTB/POZ domain, but differ in their C-terminal region, most containing C-terminal FLYWCH zinc finger motifs. The FLYWCH domain in Mod proteins has a putative role in protein-protein interactions; for example, Mod-67.2 interacts with DNA-binding protein Su via its FLYWCH domain.
FLYWCH domains have been described in other proteins as well, including suppressor of killer of prune, Su, which contains 4 terminal FLYWCH zinc finger motifs in a tandem array and a C-terminal glutathione S-transferase domain.