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. 2023 Feb 16;51(5):2434–2446. doi: 10.1093/nar/gkad081

Figure 4.

Figure 4.

Predicted structure of the C-terminal region of CeMETT10. (A) Structure of the C-terminal KA-1 domain of human METTL16 (PDB: 6M1U) (35). The disordered loop (dashed line) is inserted between KA-1a (magenta) and KA-1b (green). (B) Model structures of the C-terminal regions of CeMETT10 and hMETTL16 homologs from invertebrates [Caenorhabditis elegans (MET16_CAEEL), Octopus vulgaris (A0A6P7TIF1_OCTVU), Tetranychus urticae (T1JVZ0_TETUR), Actinia tenebrosa (A0A6P8ITS0_ACTTE), and Amphimedon queenslandica (A0A1 × 7U5N0_AMPQE)], and a fission yeast [Schizosaccharomyces pombe (MTL16_SCHPO)] generated by Alphafold2 (44,45). The disordered region between KA-1a (magenta) and KA-1b (green), predicted by Alphafold2 in each structure, is depicted by dashed lines (Supplementary Figures 2, 6). The arginine-rich region, RRR, is colored blue. (C) Alignments of the amino acid sequences of the C-terminal regions of hMETTL16 and CeMETT10. The secondary structural elements (α-helices and β-strands) for hMETTL16 and CeMETT10 are shown in parallel above and below the alignment, respectively.