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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS (By similarity). ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro) Homodimer. Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain. Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.