DNA-binding domain of MAX gene-associated protein and related T-box proteins
MGA (also known as MGAP, MAX dimerization protein, MAD5, MXD5) is a dual-specificity transcription factor that regulates the expression of both, MAX-network and T-box family target genes. MGA functions as a repressor or an activator; it binds to 5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence. Its function is activated by heterodimerization with MAX. This subfamily belongs to the T-box family of transcription factors which play a multitude of diverse functions throughout development. The founding member of the T-box family is Brachyury (also known as TBXT, or T). T-box family members share a conserved DNA-binding domain (T-box) which binds DNA in a sequence-specific manner. Common features shared by T-box family members are DNA-binding and transcriptional regulatory activity, a role in development, and conserved expression patterns.
Feature 1:DNA binding site [nucleic acid binding site]
Evidence:
Comment:based on related T-box transcription factors bound with DNA
Comment:T-box monomers dimerize upon DNA binding; some form weak dimers, others tight dimers, some may bind as non-associating monomers where the dimer is kept in register by the DNA
Jiyao W et al.(2023). "The conserved domain database in 2023.",