Fig 4.

Sequence alignment of aKMT homologs from Crenarchaea (genera preceded by a C), Euryarchaea (A), Bacteria (B), and Eukarya (E). Sequences are from Sulfolobus islandicus M.14.25 (gi|227827841), Desulfurococcus kamchatkensis 1221n (gi|218884617), Thermosphaera aggregans DSM 11486 (gi|296243046), Pyrolobus fumarii 1A (gi|347524257), Thermofilum pendens Hrk 5 (gi|119719282), Thermoproteus neutrophilus V24Sta (gi|171185324), Salinibacter ruber M8 (gi|294507034), Nostoc sp. PCC 7120 (gi|17229012), Acidilobus saccharovorans 345-15 (gi|302349255), Methanobacterium sp. SWAN-1 (gi|333987018), Pinus radiate (gi|361066863), Volvox carteri f. nagariensis (gi|302837301), Gallus gallus (gi|363739652), Danio rerio (gi|165972475), Xenopus laevis (gi|148225045), Homo sapiens (gi|154240720), Drosophila mojavensis (gi|195113923), Fervidicoccus fontis Kam940 (gi|385805356), Methanopyrus kandleri AV19 (gi|20093891), Streptomyces roseosporus NRRL 15998 (gi|291445786), and Bacillus cereus 03BB108 (gi|196045290). The amino acids that are conserved or have similar properties are shown in red letters. Region I includes the putative active site residues. The invariant amino acid residues responsible for SAM binding (region II) are shown in white letters against a red background.