Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC50926TRAM domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC50926
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.
-------------------------------------------------------------------------------
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). | |
| PubMed ID | 11313137 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.