Snake venom metalloproteases (SVMPs) embodies zinc-dependent multidomain enzymes responsible for a relevant pathophysiology in envenomation, including local and systemic hemorrhagic. The molecular features responsible for hemorrhagic potency has been associated with their multidomains structures which can target them to several receptors of different tissues and cellular types. BjussuMP-I has been characterized as a P-III hemorrhagic metalloprotease. The complete cDNA sequence of BjussuMP-I with 1540 bp encoded open reading frames of 547 amino acid residues which conserved the common domains of P-III high molecular weight hemorrhagic metalloproteases: (i) pre-pro-peptide, (ii) metalloprotease, (iii) disintegrin-like and (iv) rich cysteine domain. BjussuMP-I induced lyses in fibrin clots after 12 h incubation and inhibited collagen- and ADP-induced platelet aggregation. We are regarding, for the first time, the primary structure of an RGD-P-III class snake venom metalloprotease. A phylogenetic analysis of the BjussuMP-I metalloprotease/catalytic domain was performed to get new insights into the molecular evolution of the metalloproteases. A theoretical model of this domain was built through the combination of folding recognition (threading) techniques with a molecular dynamics simulation. Then, the final BjussuMP-I catalytic domain model was compared with other SVMPs and Reprolysin family proteins in order to identify eventual structural differences, which could help to understand the biochemical activities of these enzymes. The presence of large hydrophobic areas and some conserved surface charge-positive residues were identified as important features of the SVMPs and other metalloproteases.