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The TRAM (after TRM2 and miaB) domain is a 60-70-residue-long module that is
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-
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 .
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.
September 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Anantharaman V., Koonin E.V., Aravind L.
TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes.
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