Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro) (PubMed:25817387, PubMed:27798837). Functions in trans to edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro) (PubMed:14663147). Has no activity on correctly charged Pro-tRNA(Pro) or Ala-tRNA(Ala) (PubMed:14663147). ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro) Inhibited by the quinazolinone-based compound febrifugine from the Chinese plant Dichroa febrifuga which is used to treat malaria-associated fever (PubMed:25817387, PubMed:27798837). Also inhibited by febrifugine derivatives such as halofuginone (PubMed:25817387, PubMed:27798837). Homodimer. Expressed during the asexual blood stage including at the ring stage and in trophozoites and schizonts (at protein level). Consists of four domains: the N-terminal editing domain, the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension (Probable). The first domain (about residues 1-163) is required for editing of incorrectly charged tRNA (PubMed:14663147). When it is deleted the enzyme shows pronounced misacylation of tRNA(Pro) with alanine (PubMed:14663147). Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily.