The complete amino acid sequence of canine miniplasminogen (Mr 36,678, 333 residues) was determined with the aid of fragments obtained by cleavage with BNPS-skatole, cyanogen bromide or clostripain. The fragments were aligned with overlapping sequences. Sequence comparison with miniplasminogens of other species gave identities in the range of 80% (bovine) and 88% (human), indicating the presence of the same structural and functional domains as in the other species. Sequence comparison of different miniplasminogens showed that plasminogens of species activated by streptokinase have identical residues in positions 49, 83 and 161 of the plasmin light chain. The triad of these amino acids may represent at least one of eventually several prerequisites for the interaction and activation of plasminogen with streptokinase.