Laccases are ligninolytic enzymes that play a crucial role in various biological processes of filamentous fungi, including fruiting-body formation and lignin degradation. Lignin degradation is a complex process and its degradation in is greatly affected by the availability of oxygen. Here, a total of six putative laccase genes () were identified from the 20R-7-F01 genome. These genes, which include three typical Cu-oxidase domains, can be classified into three groups based on phylogenetic analysis. showed distinct intron-exon structures and conserved motifs, suggesting the conservation and diversity of in gene structures. Additionally, the number and type of cis-acting elements, such as substrate utilization-, stress-, cell division- and transcription activation-related cis-elements, varied between genes, suggesting that the transcription of laccase genes in 20R-7-F01 could be induced by different substrates, stresses, or other factors. The SNP analysis of resequencing data demonstrated that the of inhabiting deep subseafloor sediments were significantly different from those of inhabiting terrestrial environments. Similarly, the large variation of conserved motifs number and arrangement of laccase between subseafloor and terrestrial strains indicated that had a diverse structure. The expression of and genes was significantly up-regulated in lignin/lignite medium, suggesting that these two laccase genes might be involved in fungal utilization and degradation of lignite and lignin under anaerobic conditions. These findings might help in understanding the function of laccase in white-rot fungi and could provide a scientific basis for further exploring the relationship between the LAC family and anaerobic degradation of lignin by .

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9393519PMC
http://dx.doi.org/10.3389/fmicb.2022.923451DOI Listing

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