Targeting Echinococcus multilocularis PIM kinase for improving anti-parasitic chemotherapy
Fig 4
Domain structure and homologies of EmCDC25.
(A) Amino acid sequence alignment of the Rhodanese homology domains of EmCDC25 (EmCdc25), two S. mansoni CDC25 orthologs (SmCDC25A, SmCDC25B), and three human CDC25 orthologs (HsCDC25A-C). Conserved Rhodanese domain DCR motifs and the active site are indicated. Residues identical to EmCDC25 are shown in black on grey. (B) Phylogenetic tree based on Rhodanese domains of different CDC25-like phosphatases. Sequences derived from E. multilocularis (EmCDC25), S. mansoni (SmCDC25A/B), H. sapiens (HsCDC25A-C), C. elegans (CeCDC25 1–4), D. melanogaster (TEW, STG), and Saccharomyces cerevisiae (MIH1). Statistical method for the tree was maximum likelihood (ML), substitution model was Jones-Taylor-Thompson, ML heuristic method was Nearest Neighbour Interchange. (C) Domain structures of EmCDC25, two different CDC25 orthologs of S.mansoni (SmCDC25A/B), and three human CDC25 isoforms (HsCDC25A-C). Shown are Rhodanese domains and M-phase inducer phosphatase domains, which are typical for mammalian isoforms.