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PROSITE documentation PDOC50926

TRAM domain profile


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.

Last update:

September 2003 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

TRAM, PS50926; TRAM domain profile  (MATRIX)


1AuthorsAnantharaman V., Koonin E.V., Aravind L.
TitleTRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes.
SourceFEMS Microbiol. Lett. 197:215-221(2001).
PubMed ID11313137

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