Background　Laccases　are　green　biocatalysts　with　wide　industrial　applications.　The　study　of　efficient　and　specific　laccase　producers　remains　a　priority.　Cerrena　species　have　been　shown　to　be　promising　basidiomycete　candidates　for　laccase　production.　Although　two　sets　of　Cerrena　genome　data　have　been　publicly　published,　no　comprehensive　bioinformatics　study　of　laccase　gene　family　in　C.　unicolor　has　been　reported,　particularly　concerning　the　analysis　of　their　three-dimensional　(3D)　structures　and　molecular　docking　to　substrates,　like　ABTS　and　aflatoxin　B1　(AFB1).　Results　In　this　study,　we　conducted　a　comprehensive　genome-wide　analysis　of　laccase　gene　family　in　C.　unicolor　87613.　We　identified　eighteen　laccase　genes　(CuLacs)　and　classified　them　into　three　clades　using　phylogenetic　analysis.　We　characterized　these　laccases,　including　their　location　in　contig　5,6,9,12,15,19,26,27,　gene　structures　of　different　exon-intron　arrangements,　molecular　weight　ranging　from　47.89　to　141.41　kDa,　acidic　pI　value,　5-15　conserved　protein　motifs,　signaling　peptide　of　extracellular　secretion　(harbored　by　13　CuLacs)　and　others.　In　addition,　the　analysis　of　cis-acting　element　in　laccase　promoters　indicated　that　the　transcription　response　of　CuLac　gene　family　was　regulatable　and　complex　under　different　environmental　cues.　Furthermore,　analysis　of　transcription　pattern　revealed　that　CuLac8,　12　and　CuLac2,　13　were　the　predominant　laccases　in　response　to　copper　ions　or　oxidative　stress,　respectively.　Finally,　we　focused　on　the　3D　structure　analysis　of　CuLac　proteins.　Seven　laccases　with　extra　transmembrane　domains　or　special　sequences　were　particularly　interesting.　Predicted　structures　of　each　CuLac　protein　with　or　without　these　extra　sequences　showed　altered　interacting　amino　acid　residues　and　binding　sites,　leading　to　varied　affinities　to　both　ABTS　and　AFB1.　As　far　as　we　know,　it　is　the　first　time　to　discuss　the　influence　of　the　extra　sequence　on　laccase＇s　affinity　to　substrates.　Conclusions　Our　findings　provide　robust　genetic　data　for　a　better　understanding　of　the　laccase　gene　family　in　C.　unicolor　87613,　and　create　a　foundation　for　the　molecular　redesign　of　CuLac　proteins　to　enhance　their　industrial　applications.