Forkhead-associated domain
| FHA domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
solution structure of the fha domain of human ubiquitin ligase protein rnf8 | |||||||||
| Identifiers | |||||||||
| Symbol | FHA | ||||||||
| Pfam | PF00498 | ||||||||
| Pfam clan | CL0357 | ||||||||
| InterPro | IPR000253 | ||||||||
| PROSITE | PDOC50006 | ||||||||
| SCOP2 | 1qu5 / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, the forkhead-associated domain (FHA domain) is a phosphopeptide recognition domain found in many regulatory proteins. It displays specificity for phosphothreonine-containing epitopes but will also recognise phosphotyrosine with relatively high affinity. It spans approximately 80-100 amino acid residues folded into an 11-stranded beta sandwich, which sometimes contains small helical insertions between the loops connecting the strands.
To date, genes encoding FHA-containing proteins have been identified in bacterial, eukaryotic and archaeal genomes. The domain is present in a diverse range of proteins, such as kinases, phosphatases, kinesins, transcription factors, RNA-binding proteins, and metabolic enzymes which partake in many different cellular processes - DNA repair, signal transduction, vesicular transport, and protein degradation are just a few examples.