Figure 4From: Quod erat demonstrandum?The mystery of experimental validation of apparently erroneous computational analyses of protein sequencesMultiple alignment of predicted archaeal thymidylate synthases (TS). The scheme for displaying multiple alignments is as described in the legend to Figure 1. Residues are colored at 90% consensus. A consensus secondary structure was derived using known TS structures from R. norvegicus, E. coli and bacteriophage T4 deoxycytidylate hydroxymethyltransferase (1B5D). The Archaeoglobus fulgidus TS has a duplication of the TS domain and the amino-terminal domain (N.TS_Af; shaded gray) is predicted to be inactive. Af, Archaeoglobus fulgidus; At, Arabidopsis thaliana; BPSP1; bacteriophage SP1; Bs, B. subtilis; Dm, Drosophila melanogaster; Dr, D. radiodurans; Ec, E. coli; Mj, M. jannaschii; Mt, M. tuberculosis; Mth, M. thermoautotrophicum; Nm, Neisseria meningitidis; Rn, R. norvegicus; T2, bacteriophage T2; Xf, Xylella fastidiosa.Back to article page