A　novel　laccase　gene　Lac1　and　its　cDNA　were　cloned　from　a　white-rot　fungus　Cerrena　sp.　and　characterized.　The　1554-bp　cDNA　of　Lac1　encoded　a　mature　protein　with　497　amino　acids,　preceded　by　a　signal　peptide　of　20　amino　acids.　An　unconventional　intron　splice　site　and　incomplete　splicing　variants　of　Lac1　were　observed.　Lac1　was　heterologously　expressed　in　the　yeast　host　Pichia　pastoris,　and　a　maximal　laccase　activity　of　6.3UmL-1　in　the　fermentation　broth　was　achieved　after　fermentation　for　9　days.　The　recombinant　protein　rLac1　was　purified,　and　its　enzymatic　properties　and　functional　characteristics　were　investigated.　When　ABTS　was　used　as　the　substrate,　the　enzyme　was　most　active　at　pH　3.5　and　55°C,　and　stable　at　pH　4-10　and　20-60°C.　The　Km　and　kcat　values　of　rLac1　toward　ABTS　were　28.9　μM　and　332.4s-1,　respectively.　Furthermore,　rLac1　was　tolerant　to　common　metal　ions　up　to　100mM　concentration　and　capable　of　decolorizing　structurally　different　dyes　in　the　absence　of　a　redox　mediator.　Hence,　Lac1　may　be　useful　for　industrial　applications,　such　as　dye　decolorization　and　bioremediation.　©　2015　Elsevier　B.V.