v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | 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 formationIn several other proteins associated with the translation machineryIn a family of small uncharacterised archaeal proteins that are predicted to have a role in the regulation of tRNA modification and/or translationThe 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 [].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 [ ]. |
Short Name | TRAM_dom |