The TRAM (after TRM2 and miaB) domain is a 60-70-residue-long module that is found in:

• Two distinct classes of tRNA-modifying enzymes, namely uridine methylases of the TRM2 family and enzymes of the miaB family that are involved in 2- methylthioadenine formation,
• In several other proteins associated with the translation machinery,
• In a family of small uncharacterized archaeal proteins that are predicted to have a role in the regulation of tRNA modification and/or translation.

The TRAM domain can be found alone or in association with other domains, such as the catalytic biotin/lipoate synthase-like domain, the RNA methylase domain, the ribosomal S2 domain (see <PDOC00744>) and the eIF2-β domain. The TRAM domain is predicted to bind tRNA and deliver the RNA-modifying enzymatic domain to their targets [1].

Secondary structure prediction indicates that the TRAM domain adopts a simple β barrel fold. The conservation pattern of the TRAM domain consists primarily of small and hydrophobic residues that correspond to five β-strands in the predicted secondary structure [1].

The profile we developed covers the entire TRAM domain.