Background: The relevance of bioinformatics is being realized in the era of genomics,
assisting in genome-wide identification and characterization of putative gene families of different
enzymes for diverse industrial applications. Therefore, in the present manuscript, Mn peroxidases
protein sequences from different fungal sources were subjected to bioinformatics assessment for
homology search, multiple sequence alignment, phylogenetic tree construction and motif search.
Objectives: The available protein sequences representing enzymes is being utilized to decipher the
sequence-structure-functional relationship with the aid of bioinformatics tools. In-silico
protein sequences of several industrially important enzymes with an aim to improve the catalytic
efficiency, thermostability, structural prediction and validation have been reported in recent years.
Method: A total of 78 full length protein sequences representing manganese peroxidases from diverse
fungal sources have been retrieved from GenBank and subjected to in-silico analysis for
homology search, physio-chemical attributes, multiple sequence alignment, phylogenetic tree and
motif assessments. Multiple accessions from same fungal sources like 9 accessions of Puncularia
were included to get an insight into the structural and functional diversity of the
Results: The physio-chemical attributes showed variability in the amino acid residues ranging
from 341 to 613, molecular weight from 31939.035 to 58082.9 daltons while the pI ranging from
3.8 to 5.39. Thermostability and hydrophilic nature of these proteins was predominantly observed
as revealed by comparatively high value of aliphatic index and negative value of GRAVY respectively.
The phylogenetic tree revealed distinct clusters for different fungal genus and multiple accessions
representing the same genus were grouped together indicating sequence level similarity.
Conclusion: Five motifs were uniformly observed among all the sequences and these revealed
similarities to Plant_ peroxidase_family. The plant peroxidase-like superfamily is reported to be
prevalent in three kingdoms of life and know to carry out a variety of biosynthetic and degradative