M regulator protein trans-acting positive regulator (Mga) is a DNA-binding protein that activates the expression of several important virulence genes in group A streptococcus in response to changing environmental conditions []. This domain is found in the centre of the Mga proteins. This domain is also found in a number of bacterial RofA transcriptional regulators that seem to be largely restricted to streptococci. These proteins have been shown to regulate the expression of important bacterial adhesins []. This is presumably a DNA-binding domain.
Mga is a DNA-binding protein that activates the expression of several important virulence genes in group A streptococcus in response to changing environmental conditions. It appears to contain two DNA-binding domains that are required for direct activation of the Mga virulence regulon in vivo []. This entry represents the Mga DNA binding domain, which also appears to be found in other regulatory proteins.
MAX gene-associated protein (MGA) is a dual-specificity transcription factor, acting as a repressor or an activator and binding to 5'-AATTTCACACCTAGGTGTGAAATT-3'. MGA regulates genes targeted by MYC-MAX, suppressing transcriptional activation by MYC and inhibiting MYC-dependent cell transformation. MGA binds DNA via a T-Box []. MGA is a component of the MLL1 complex [].
This domain can be found in the MAX gene-associated protein (Mga), which is a dual-specificity transcription factor that contains both a bHLHZip domain and a T-box domain and is able to bind to and regulate transcriptional targets through both E-box sites as well as T-box-binding elements (TBEs) []. MAX gene-associated protein (MGA) is a dual-specificity transcription factor, acting as a repressor or an activator and binding to 5'-AATTTCACACCTAGGTGTGAAATT-3'. MGA regulates genes targeted by MYC-MAX, suppressing transcriptional activation by MYC and inhibiting MYC-dependent cell transformation. MGA binds DNA via a T-Box []. MGA is a component of the MLL1 complex [].
Mga is a DNA-binding protein that activates the expression of several important virulence genes in group A streptococcus in response to changing environmental conditions []. This region corresponds to the PRD like region.
E2F6 is a member of the E2F family of transcription factors. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA-binding domain, a dimerisation domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumour suppressor protein association domain which is embedded within the transactivation domain. E2F6 is atypical because it lacks the transactivation and tumour suppressor protein association domains. It contains a modular suppression domain and is an inhibitor of E2F-dependent transcription. The protein is part of a multimeric protein complex that contains a histone methyltransferase and the transcription factors Mga and Max. Multiple transcript variants encoding several different isoforms have been found for this gene. In general, the E2F family plays a crucial role in the control of cell cycle and action of tumour suppressor proteins and is also a target of the transforming proteins of small DNA tumour viruses [, ]Homo sapiens Mus musculus (Mouse) Macaca fascicularis (Crab eating macaque).
