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
SCOP 1qu5
SUPERFAMILY 1qu5

In molecular biology, the forkhead-associated domain (FHA domain) is a phosphopeptide recognition domain found in many regulatory proteins.[1] 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.[2]

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.

References

  1. Hofmann K, Bucher P (September 1995). "The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors". Trends Biochem. Sci. 20 (9): 347–9. doi:10.1016/S0968-0004(00)89072-6. PMID 7482699.
  2. Durocher D, Jackson SP (February 2002). "The FHA domain". FEBS Lett. 513 (1): 58–66. doi:10.1016/S0014-5793(01)03294-X. PMID 11911881.

External links

This article incorporates text from the public domain Pfam and InterPro IPR000253

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