SMART: Pfam domain TRAM

The domain within your query sequence starts at position 500 and ends at position 574; the E-value for the TRAM domain shown below is 1e-12.

KTSVGCSQLVLVEGFSKRSTTDLCGRNDANLKVIFPDAEVEDITNPGLKVRAQPGDYVLV
KITSASSQTLKGHIL

TRAM

PFAM accession number:	PF01938
Interpro abstract (IPR002792):	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 uncharacterised 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 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 [ (PUBMED:11313137) ]. 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 [ (PUBMED:11313137) ].

PFAM accession number:

PF01938

Interpro abstract (IPR002792):

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 uncharacterised 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 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 [ (PUBMED:11313137) ]. 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 [ (PUBMED:11313137) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry TRAM