Forkhead-associated domain
| FHA domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
solution structure of the fha domain of human ubiquitin ligase protein rnf8
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| Identifiers | |||||||||
| Symbol | FHA | ||||||||
| Pfam | PF00498 | ||||||||
| Pfam clan | CL0357 | ||||||||
| InterPro | IPR000253 | ||||||||
| PROSITE | PDOC50006 | ||||||||
| SCOP | 1qu5 | ||||||||
| SUPERFAMILY | 1qu5 | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
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 eubacterial and eukaryotic but not 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.
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