Has peptidylprolyl isomerase (PPIase) and co-chaperone activities (PubMed:15664653, PubMed:15850699). Assists protein folding by catalyzing the peptidyl conversion of cis and trans rotamers of the prolyl amide bond of protein substrates (PubMed:15664653, PubMed:15850699, PubMed:23974147). Inhibits calcineurin phosphatase activity in vitro (PubMed:15850699, PubMed:17289400, PubMed:23974147). Plays an essential role in merozoite egress from host erythrocytes (PubMed:15664653, PubMed:23974147). [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Inhibited by FK506 and its derivates, such as ascomycin, and rapamycin (PubMed:15664653, PubMed:15850699). FK506 and rapamycin inhibit peptidylprolyl isomerase activity but not chaperone activity (PubMed:15664653). Inhibited by N-(2-ethyl-phenyl)-2-(3H-imidazao [4, 5-b] pyridin-2-yl-sulfanyl)-acetamide (D44) (PubMed:23974147). Not inhibited by cyclosporin A (PubMed:15664653, PubMed:15850699). Inhibition of calcineurin phosphatase activity is enhanced by FK506 (PubMed:15850699). Homodimer (PubMed:17289400). Interacts (via TPR repeats) with HSP90 (probably via MEEVD motif) (PubMed:15850699, PubMed:19691130). During the asexual blood stage, predominantly localizes to the cytoplasm of ring stage parasites and then translocates to the nucleus during the differentiation into trophozoites and schizonts. Expressed during all parasite blood stages (at protein level). The PPIase FKBP-type domain contributes to the chaperone activity (PubMed:15664653). Required for the inhibition of calcineurin phosphatase activity (PubMed:15850699). The TPR repeats are important for the chaperone activity (PubMed:15664653). In another study, these repeats appear to be dispensable for chaperone activity (PubMed:15850699). Dispensable for PPIase activity (PubMed:15850699). Dispensable for the inhibition of calcineurin phosphatase activity (PubMed:15850699). Belongs to the FKBP-type PPIase family.