An Atlas of the Thioredoxin Fold Class Reveals the Complexity of Function-Enabling Adaptations
Figure 9
Transitive similarity relationships link the thioredoxins and the peroxiredoxins.
A Subset of the sequence similarity network from Fig. 4, with nodes colored according to the identity of the amino acid predicted to occcupy the position of the cis-proline at the N-terminus of beta strand 3 in the Trx fold (Pro 75 in human Trx 1). The orange path traces transitive sequence similarity relationships between human Trx 2, passing through B. japonicum CMP (CYCY_BRAJA), and ending at bovine Prx 3 (PRDX3_BOVIN). Large nodes represent sequences that are associated with the structures from Fig. 3. Predictions are based on sequence alignments to PFAM Thioredoxin-like Clan HMMs. B The same path—connecting the structures associated with the sequences in A—traced through a subset of the structure-based network from Fig. 3B. C The same path traced through a subset of the structure-based hierarchical clustering of representative structures from Fig. 3D.