<p>The TRAM (after TRM2 and miaB) domain is a 60-70-residue-long module that is found in:<ul><li>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</li><li>In several other proteins associated with the translation machinery</li><li>In a family of small uncharacterised archaeal proteins that are predicted to have a role in the regulation of tRNA modification and/or translation</li></ul>The TRAM domain can be found alone or in association with other domains, such as the catalytic biotin/lipoate synthetase-like domain, the RNA methylase domain, the ribosomal S2 domain and the eIF2-beta domain. The TRAM domain is predicted to bind tRNA and deliver the RNA-modifying enzymatic domain to their targets [<cite idref="PUB00009729"/>].Secondary structure prediction indicates that the TRAM domain adopts a simple beta-barrel fold. The conservation pattern of the TRAM domain consists primarily of small and hydrophobic residues that correspond to five beta-strands in the predicted secondary structure [<cite idref="PUB00009729"/>].</p> Deoxyribonuclease/rho motif-related TRAM