An extracellular laccase-producing ascomycete was isolated from soil and identified as Paraconiothyrium variabile using rDNA sequence analysis. Typical laccase substrates including 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS), 2,6-dimethoxyphenol (DMP), and guaiacol were oxidized by the purified enzyme (designated as PvL). The molecular mass of PvL was 84kDa and it showed a pI value of 4.2. The enzyme acted optimally at pH 4.8 and exhibited an optimum temperature of 50°C. Using ABTS, PvL represented K_m and V_max of 203μM and 40μmolmin⁻¹mg⁻¹, respectively. After 24h incubation at pH 4.8 and 4°C, 80% of the initial activity of PvL remained. The enzyme was inhibited by Fe²⁺, Hg²⁺, and Mn²⁺, but induced by Cu²⁺. EDTA (10mM), 1,4-dithiothreitol (DTT) (0.1mM), and NaN₃ (10mM) were found to completely inhibit PvL. Sixty-eight percent of Malachite green was decolorized by 4U/mL of PvL after 15min incubation at 30°C.