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:
| FLYWCH zinc finger domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | FLYWCH | ||||||||
| Pfam | PF04500 | ||||||||
| Pfam clan | CL0274 | ||||||||
| InterPro | IPR007588 | ||||||||
| |||||||||
F/Y-X(n)-L-X(n)-F/Y-X(n)-WXCX(6-12)CX(17-22)HXH
where X indicates any amino acid. This domain was first characterised in Drosophila modifier of mdg4 proteins, Mod(mgd4), putative chromatin modulators involved in higher order chromatin domains. Mod(mdg4) proteins share a common N-terminal BTB/POZ domain, but differ in their C-terminal region, most containing C-terminal FLYWCH zinc finger motifs.[1] The FLYWCH domain in Mod(mdg4) proteins has a putative role in protein-protein interactions; for example, Mod(mdg4)-67.2 interacts with DNA-binding protein Su(Hw) via its FLYWCH domain.
FLYWCH domains have been described in other proteins as well, including suppressor of killer of prune, Su(Kpn), which contains 4 terminal FLYWCH zinc finger motifs in a tandem array and a C-terminal glutathione S-transferase (GST) domain.[2]
References
edit- ^ Dorn R, Krauss V (March 2003). "The modifier of mdg4 locus in Drosophila: functional complexity is resolved by trans splicing". Genetica. 117 (2–3): 165–77. doi:10.1023/A:1022983810016. PMID 12723696. S2CID 6305770.
- ^ Provost E, Shearn A (August 2006). "The Suppressor of Killer of prune, a unique glutathione S-transferase". Journal of Bioenergetics and Biomembranes. 38 (3–4): 189–95. doi:10.1007/s10863-006-9034-1. PMID 16944302. S2CID 27833572.