Extended Data Fig. 5: The potential key catalytic site of TRMT61A. | Nature Cancer

Extended Data Fig. 5: The potential key catalytic site of TRMT61A.

From: TRMT6-mediated tRNA m1A modification acts as a translational checkpoint of histone synthesis and facilitates colorectal cancer progression

Extended Data Fig. 5

(a) Sequence alignment of the MTase domain of TRMT61A across multiple species. Strictly conserved residues are highlighted with red boxes, emphasizing key regions of evolutionary conservation. The sequence alignment was conducted using the Clustal Omega tool available from the EBI website (https://www.ebi.ac.uk/). (b) An overview of the core residues involved in substrate binding within the MTase domain of TRMT61A. The three conserved residues identified from the sequence alignment are highlighted in red text (Ser114, Glu135, Asp181), and all three are substrate-binding residues. The 3D structure of the MTase domain was obtained from the Protein Data Bank (PDB: 5CCB, https://www.rcsb.org/3d-view/5CCB/1?preset=symmetry&sele=0).

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