Haolt: Fig. 1. Comparison of conserved regions in the SET‐domain between OsSET1 and selected representative proteins. A sequence alignment of SET‐N and SET‐C of the SET domain and the lengths of the variable insert regions (SET‐I) were indicated. Ident

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Fig. 1. Comparison of conserved regions in the SET‐domain between OsSET1 and selected representative proteins. A sequence alignment of SET‐N and SET‐C of the SET domain and the lengths of the variable insert regions (SET‐I) were indicated. Identical residues were shaded in black and conservative changes were shaded in grey. The putative conserved secondary structural elements were roughly indicated above the sequence alignment, in which arrows refer to β strands and bold bars refer to α helices. Regions putatively involved in binding to the cofactor product AdoHcy were indicated with green, and other three highly conserved sequence regions (the last two of which form the unusual knot structure) were indicated with a blue bar below the aligned sequences. The invariant tyrosine residue implicated to function as a general base for catalysis was indicated with a black triangle below the alignment. No CLC and CRC conservative sequences were found in Post‐SET region of OsSET1. DDBJ/EMBL/GenBank accession numbers: DIM‐5_Nc (AAL35215), SET7/9_Hs (AAL56579), Clr4_Sp (CAA07709), SET1_Os (AAK28975), OsSET1_Os (AAN01115), RubiscoLs (AAA69903).

File:Haolt-F1.large.jpg - Revision history

Haolt: Fig. 1. Comparison of conserved regions in the SET‐domain between OsSET1 and selected representative proteins. A sequence alignment of SET‐N and SET‐C of the SET domain and the lengths of the variable insert regions (SET‐I) were indicated. Ident