{PDOC50926}
{PS50926; TRAM}
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* TRAM domain profile *
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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-beta 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
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 [1].

The profile we developed covers the entire TRAM domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2003 / First entry.

[ 1] Anantharaman V., Koonin E.V., Aravind L.
     "TRAM, a predicted RNA-binding domain, common to tRNA uracil
     methylation and adenine thiolation enzymes."
     FEMS Microbiol. Lett. 197:215-221(2001).
     PubMed=11313137

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