EC Number   |
Subunits |
Reference |
|---|
   2.1.1.220 | More |
in mitochondria, MTase Trmt61B forms a tetramer, presumed to resemble the homotetramers of TrmI proteins. In support of a similar structural arrangement between Trmt61B and TrmI, a phylogenetic analysis confirmed a bacterial origin of the human protein |
756160 |
| 2.1.1.220 | More |
Trm6 is less conserved with respect to TrmI than Trm61 and lacks a cofactor-binding pocket, enzyme quaternary structure, overview |
736642 |
| 2.1.1.220 | More |
two subunit types, TRM6 or TRM61 |
721024 |
| 2.1.1.220 | tetramer |
4 * 28582, calculation from sequence, composed of two types of subunits (Gcd14p and Gcd10p) |
-, 660026 |
| 2.1.1.220 | tetramer |
dimer of heterodimers in which each heterodimer comprises a catalytic chain, Trm61, and a homologous but noncatalytic chain, Trm6, repurposed as a tRNA-binding subunit that acts in trans, crystal structure analysis |
736642 |
| 2.1.1.220 | tetramer |
dimers of tightly assembled dimers, bacterial enzymes from thermophilic organisms display additional intermolecular ionic interactions across the dimer interfaces, interactions and structure analysis, overview |
719192 |
| 2.1.1.220 | tetramer |
dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, and the tetramer is strengthened by four intersubunit disulfide bridges, interactions and structure analysis, overview |
719192 |
| 2.1.1.220 | tetramer |
dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, interactions and structure analysis, overview |
719192 |
| 2.1.1.220 | tetramer |
dimers of tightly assembled dimers, interactions and structure analysis, overview |
719192 |
| 2.1.1.220 | tetramer |
the enzyme remains tetrameric upon tRNA binding, with formation of complexes involving one to two molecules of tRNA per TrmI tetramer |
699528 |
