|PROSITE documentation PDOC51703 [for PROSITE entry PS51703]|
Nuclear factors NF90 and NF45 form a protein complex involved in a variety of cellular processes and are thought to affect gene expression both at the transcriptional and translational level. In addition, this complex affects the replication of several viruses through direct interactions with viral RNA. NF90 and NF45 dimerize through their common DZF domain. The DZF domain shows structural similarity to the template-free nucleotidyltransferase family of RNA modifying enzymes. However, the lack of conserved catalytic residues suggests that the DZF domain encodes a 'pseudotransferase' that is no longer able to catalyze transfer of nucleotides.
The DZF dimerization domain form an oblong structure with a flat face on one side and a curved face on the other. The DZF domain is bipartite and characterized by an N-terminal mixed α-β region that contains a central anti-parallel β-sheet and a C-terminal α-helical region (see <PDB:4AT7>). The overall structure has a pseudo two-fold rotational symmetry. The central β-sheet forms the base of a cleft between the N- and C-terminal halves while dimerization is mediated by the α-helices at the C-terminus .
The profile we developed covers the entire DZF domain.Last update:
February 2014 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Parker L.M. Fierro-Monti I. Mathews M.B.|
|Title||Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase.|
|Source||J. Biol. Chem. 276:32522-32530(2001).|
|2||Authors||Doerks T. Copley R.R. Schultz J. Ponting C.P. Bork P.|
|Title||Systematic identification of novel protein domain families associated with nuclear functions.|
|Source||Genome Res. 12:47-56(2002).|
|3||Authors||Wolkowicz U.M. Cook A.G.|
|Title||NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold.|
|Source||Nucleic Acids Res. 40:9356-9368(2012).|