Protein domains are regions of proteins that are homologous, having protein sequences that remain the same throughout evolution. This confers that the region is likely important to protein structure, folding, and function [1].
Protein domain analysis of proteins can be completed using SMART or InterPro which uses information from several databases and predictive models to classify and analyze protein families. [2].
Clustal Omega alignment of FOXN1 orthologs with purple box denoting location of the forkhead box region
Discussion
Domain analysis of model organism FOXN1 orthologs using SMART revealed conservation of the Forkhead Box Domain. Not only did they all have FHDs that were 62 amino acids in length, but when they were aligned using Clustal Omega, almost all of the amino acids in this region were conserved across all model organisms (denoted by *). Because of this homology, small changes in amino acid sequence will likely cause significant dysfunction in the FOXN1 protein, specifically affecting its ability to bind to DNA as a transcription factor.
Sources
1. Wang, Y., Zhang, H., Zhong, H., & Xue, Z. (2021). Protein domain identification methods and online resources. Computational and structural biotechnology journal, 19, 1145–1153. https://doi.org/10.1016/j.csbj.2021.01.041 2. Paysan-Lafosse T, Blum M, Chuguransky S, Grego T, Pinto BL, Salazar GA, Bileschi ML, Bork P, Bridge A, Colwell L, Gough J, Haft DH, Letunić I, Marchler-Bauer A, Mi H, Natale DA, Orengo CA, Pandurangan AP, Rivoire C, Sigrist CJA, Sillitoe I, Thanki N, Thomas PD, Tosatto SCE, Wu CH, Bateman A. InterPro in 2022. Nucleic Acids Research, Nov 2022, (doi: 10.1093/nar/gkac993)
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