|PROSITE documentation PDOC50926|
The TRAM (after TRM2 and miaB) domain is a 60-70-residue-long module that is found in:
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 .
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 .
The profile we developed covers the entire TRAM domain.Last update:
September 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Anantharaman V., Koonin E.V., Aravind L.|
|Title||TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes.|
|Source||FEMS Microbiol. Lett. 197:215-221(2001).|