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. Author manuscript; available in PMC: 2010 Aug 19.
Published in final edited form as: J Am Chem Soc. 2009 Aug 19;131(32):11581–11589. doi: 10.1021/ja904318w

Figure 2.

Figure 2

B-block histidine is the most conserved residue in the intein sequences. Structure-based multiple sequence alignment of ΔΔIhh-SM and other inteins was achieved the using DALI server. ΔΔIhh-SM is an engineered and minimized Mtu RecA intein (see text). The locations of the conserved blocks A, B, F, and G are indicated above the sequences and the corresponding residues are colored in yellow. The conserved histidines are colored in magenta while other key residues are colored in cyan. H73, H429, H439 are the conserved B-block, F-block and penultimate histidines, respectively. The first C-extein residue is colored in green. The gap (▼;) in the residue numbering for ΔΔIhh-SM results from the deletion of the endonuclease domain of Mtu RecA intein.