Pycnoporus cinnabarinus is a plant pathogen. It is common in many areas and is widely distributed throughout the world. Laccases of are some of the few oxidoreductases commercialized as industrial catalysts. In the present study, some characters of the amino acid sequence of P.cinnabarinus laccase (Lac1) were predicted and analyzed with the tools of bioinformatics. These results showed that the protein was composed of 20 kinds of amino acid; the theoretical pI of manganese peroxidase was 4.81 and the theoretical molecular weight of manganese peroxidase was 56292.0 Da; total number of atoms was 7806; the extinction coefficient was 58120 (280 nm). The N-terminal of the sequence considered was M (Met) and the estimated half-life was 30 hours (mammalian reticulocytes, in vitro). The instability index (II) was computed to be 34.50; this classifies the protein as stable. Aliphatic index was 82.64. Grand average of hydropathicity (GRAVY) was -0.063. There were 8 glycosylation sites, a signal peptide and conserved domains.