Abstract
DHHC palmitoyltransferases (DHHC-PATs) are very peculiar in that, outside the DHHC domain, they are very divergent even across orthologs from closely related species. This represents a challenge for the bioinformatic analyses of these proteins. Sequence-based analyses and predictions require a valid sequence alignment, which for this family of proteins requires extensive manual curation and this is difficult to attain for the nonspecialist. Here we present a simple method for the in silico analysis of the sequence of a particular PAT, that would allow for the identification of important structural features and functional residues in a PAT or PAT family.
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Acknowledgments
We thank Dr. Agustín Carbajal and Consuelo Coronel for testing the method described in this work and critical discussion of the manuscript.
Funding: This work was funded by grants from the Argentinian Ministry of Science and technology (MINCyT) (PICT 2013 0288 and PICT 2015 1316) and by Córdoba National University. RQ and JVT are career researchers at the National Research Council of Argentina (CONICET).
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Quiroga, R., Valdez Taubas, J. (2019). Bioinformatic Identification of Functionally and Structurally Relevant Residues and Motifs in Protein S-Acyltransferases. In: Linder, M. (eds) Protein Lipidation. Methods in Molecular Biology, vol 2009. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9532-5_15
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DOI: https://doi.org/10.1007/978-1-4939-9532-5_15
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