| Type: | Domain | Name: | G-box binding protein, multifunctional mosaic region |
| Description: | This region is often found to the N terminus of the basic-leucine zipper domain (). It is between 150 and 200 amino acids in length. The N-terminal half of this domain is rich in proline residues and has been termed the PRD (proline rich domain) [], whereas the C-terminal half is more polar and has been called the MFMR (multifunctional mosaic region). According to their motif composition, proteins containing this domain can be classified into three sub-families called A, B and C []. It has been suggested that some of these motifs may be involved in mediating protein-protein interactions []. The MFMR region contains a nuclear localisation signal in bZIP opaque and GBF-2 []. The MFMR also contains a transregulatory activity in TAF-1. The MFMR in CPRF-2 contains cytoplasmic retention signals []. | Short Name: | MFMR |
