Thiol protease that cleaves dipeptides from the N-terminus of protein substrates (PubMed:15304495, PubMed:20833209). Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids (PubMed:20833209). Proline cannot occupy the P1 position and arginine or lysine cannot occupy the P2 position of the substrate (PubMed:20833209). Involved in host hemoglobin degradation by generating dipeptides from hemoglobin-derived oligopeptides (PubMed:15304495). Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro. Binds 1 Cl(-) ion per heavy chain. Optimum pH is 6-6.5. Monomer. In schizonts, the immature form localizes to the parasitophorous vacuole (PubMed:15304495). In trophozoites, the mature form localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested (PubMed:15304495). Expressed during the asexual blood stage including in trophozoites and schizonts (at protein level). Belongs to the peptidase C1 family.