Extended Data Fig. 1: Alignment of TET homologues in C. reinhardtii with Naegleria Tet1. | Nature

Extended Data Fig. 1: Alignment of TET homologues in C. reinhardtii with Naegleria Tet1.

From: A vitamin-C-derived DNA modification catalysed by an algal TET homologue

Extended Data Fig. 1: Alignment of TET homologues in C. reinhardtii with Naegleria Tet1.The alternative text for this image may have been generated using AI.

Eight TET-like proteins were found using the TET–JBP domain as a query for BLAST search in the Phytozome database of C. reinhardtii. These proteins have a conserved His-X-Asp motif, as observed in TET proteins from mammals and Naegleria. The symbols above the sequence denote the functional residues in N. gruberi (Ng)Tet1 determined by structural and biochemical analyses. m, metal (iron) binding site; C, 5mC interaction; a, active centre; α, 2-OG binding site, which is not conserved in CrTET1 (CMD1). The gene names for the CrTET in the Phytozome database are as follows: CrTET1: Cre12.g553400, CrTET2: Cre16.g654100, CrTET3: Cre02.g081150, CrTET4: Cre02.g141466, CrTET5: Cre17.g734757, CrTET6: Cre15.g643388, CrTET7: Cre02.g142867, CrTET8: Cre15.g642800.

Back to article page