Fig. 5
Secondary structure prediction of the PhaC2 polymerase in Cobetia sp. MC34. A The PSIPRED modeling plot predicts a high proportion of strand and helix secondary structures in the N-terminal (amino acids 1 to 674), whereas the extended C-terminus (amino acid 614 to 993) is predicted to consist primarily of unordered coiled domains, short helixes, and one strand domain. B The second PSIPRED plot shows an abundance of small non-polar and polar amino acids in the extended C-terminus including the positively charged lysine and arginine residues. C A generalized structure of the Cobetia sp. MC34 PhaC2 protein. The catalytic region is homologous to class I PhaC polymerases and contains an N-terminal PHA_synth_I domain and a SYCIG l PhaC box. The extended C-terminus (380 amino acids) has an unordered structure with a computed pI of 10.34.