Figure 1

Secondary structure of aaTHEP1 and multiple sequence alignment to homologous sequences. Multiple sequence alignment of aaTHEP1 with the four most homologous sequences from both, thermophiles and eukaryotes in the order as they were detected by BLAST. The aligned sequences are THEP1 from Aquifex aeolicus VF5 (aaTHEP1, accession number NP_213886), THEP1 from Thermotoga maritima MSB8 (tmTHEP1, accession number NP_227852), THEP1 from Pyrococcus horikoshii OT3 (phTHEP1, accession number NP_142728), THEP1 from Methanocaldococcus jannaschii DSM 2661, accession number NP_248567), THEP1 from Pyrococcus furiosus DSM 3638 (accession number NP_578230), THEP1 from Mus musculus (mmTHEP1, accession number NP_079912), THEP1 from Danio rerio (drTHEP1, accession number NP_001003463), THEP1 from Rattus norvegicus (rnTHEP1, accession number XP_341723) and THEP1 from Homo sapiens (hsTHEP1, accession number NP_115700). The secondary structure of aaTHEP1 as calculated by DSSP and the locations of the Walker A (P-loop) and Walker B motif are shown with reference to the aaTHEP1 sequence. Six amino acids that could not be resolved are indicated by a white box (n. r.). Conservation of residues by 100%, 80% and 60% are coloured red, orange and yellow, respectively.