FLYWCH zinc finger

{{Infobox protein family

| Symbol = FLYWCH

| Name = FLYWCH zinc finger domain

| image =

| width =

| caption = solution structure of the fifth flywch domain of flywch-type zinc finger-containing protein 1

| Pfam = PF04500

| Pfam_clan = CL0274

| InterPro = IPR007588

| SMART =

| PROSITE =

| MEROPS =

| SCOP =

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

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(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.{{cite journal | vauthors = Dorn R, Krauss V | title = The modifier of mdg4 locus in Drosophila: functional complexity is resolved by trans splicing | journal = Genetica | volume = 117 | issue = 2–3 | pages = 165–77 | date = March 2003 | pmid = 12723696 | doi = 10.1023/A:1022983810016 | s2cid = 6305770 }} 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.{{cite journal | vauthors = Provost E, Shearn A | title = The Suppressor of Killer of prune, a unique glutathione S-transferase | journal = Journal of Bioenergetics and Biomembranes | volume = 38 | issue = 3–4 | pages = 189–95 | date = August 2006 | pmid = 16944302 | doi = 10.1007/s10863-006-9034-1 | s2cid = 27833572 }}