Bioinformatic analysis of domain and motif architecture of cellulase enzymes in five CAZy families of Ascomycota

Articles in Press

Document Type : Data Analysis

Authors

1 Department of Plant Protection. Faculty of Crop Sciences, Sari Agricultural Sciences and Natural Resources University (SANRU), Sari, Iran

2 Nuclear Agriculture Research School, Nuclear Science and Technology Research Institute (NSTRI), Karaj, Iran

Abstract

Cellulase enzymes degrade cellulose, the most abundant structural polysaccharide in plant biomass, thereby playing a central role in fungal ecology and biotechnology. Here, we conducted a bioinformatic analysis of cellulase enzymes across the phylum Ascomycota to examine their diversity, domain architecture, conserved motifs, and evolutionary relationships. We retrieved cellulase protein sequences from 69 representative Ascomycota species in the UniProtKB database, analyzed them using InterProScan, COBALT, and the MEME Suite, and conducted phylogenetic reconstruction in MEGA11. Our domain analysis identified five major CAZy families: glycoside hydrolase families GH5, GH7, GH10, GH11, and auxiliary activity family AA9, demonstrating the structural diversity found in ascomycete cellulases. Motif analysis revealed multiple conserved and family-specific motifs, indicating strong conservation of catalytic cores and variability in peripheral regions. Multiple sequence alignment and phylogenetic analyses showed that cellulase proteins clustered clearly within CAZy families, with high bootstrap support, suggesting that domain and motif architectures provide robust phylogenetic signals. Together, these results clarify the structural and evolutionary diversity of ascomycete cellulases and establish a foundation for future functional, ecological, and biotechnological studies of fungal cellulases.

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References

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Mycologia Iranica

Articles in Press, Accepted Manuscript
Available Online from 30 June 2026

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  • Receive Date: 17 December 2025
  • Revise Date: 25 June 2026
  • Accept Date: 27 June 2026
  • Publish Date: 30 June 2026

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