Publication Details
Fully Automated Ancestral Sequence Reconstruction using FireProtASR
Musil Miloš, Ing., Ph.D. (DIFS)
Štourač Jan
Damborský Jiří, prof. Mgr., Dr. (UMEL)
Bednář David
and others
ancestral reconstrution, stable proteins, protein engineering, specificity
Protein evolution and protein engineering techniques are of great interest in
basic science and industrial applications such as pharmacology, medicine, or
biotechnology. Ancestral sequence reconstruction (ASR) is a powerful technique
for probing evolutionary relationships and engineering robust proteins with good
thermostability and broad substrate specificity. The following protocol describes
the setting up and execution of an automated FireProtASR workflow using
a dedicated web site. The service allows for inference of ancestral proteins
automatically, from a single protein sequence. Once a protein sequence is
submitted, the server will build a dataset of homology sequences, perform
a multiple sequence alignment (MSA), build a phylogenetic tree, and reconstruct
ancestral nodes. The protocol is also highly flexible and allows for multiple
forms of input, advanced settings, and the ability to start jobs from: (i)
a single sequence, (ii) a set of homologous sequences, (iii) an MSA, and (iv)
a phylogenetic tree. This approach automates all necessary steps and offers a way
for novices with limited exposure to ASR techniques to improve the properties of
a protein of interest. The technique can even be used to introduce catalytic
promiscuity into an enzyme. A web server for accessing the fully automated
workflow is freely accessible at https://loschmidt.chemi.muni.cz/fireprotasr/
@article{BUT168533,
author="Rayyan {Khan} and Miloš {Musil} and Jan {Štourač} and Jiří {Damborský} and David {Bednář}",
title="Fully Automated Ancestral Sequence Reconstruction using FireProtASR",
journal="Current Protocols in Bioinformatics",
year="2021",
volume="1",
number="2",
pages="1--5",
doi="10.1002/cpz1.30",
issn="1934-3396",
url="https://currentprotocols.onlinelibrary.wiley.com/doi/full/10.1002/cpz1.30"
}