Alignment of the amino acid sequences of ClPDI with other organism’s PDI and 3-D structural model. (A) Sequence alignment: ClPDI (this study), AtPDI (Arabidopsis thaliana, AY063059), HsPDI (Homo sapiens, P30101), HiPDI (Humicola insolens, AAC60578). Identical amino acids in all sequences are shaded black, conservative replacements are shaded gray. Two red boxes denote highly conserved catalytic motifs (C60GHC63, C405GHC408). Protein secondary structure was predicted by SWISS-MODEL program and represented as α helices and β strands. Underline shows the positions of the domains corresponding to domains a, b, b’ and a’. (B) A 3-D structural model of ClPDI. The structural model of the ClPDI was created based on the known crystal structure of Homo sapiens PDI (PDB: 3F8U_A) via SWISS-MODEL program and was superimposed with PDB ID: 3F8U_A (orange) to obtain structure alignment via SPDBV_4 program.