How well is enzyme function conserved as a function of pairwise sequence identity?

By Weidong Tian, Jeffrey Skolnick. 2003

433 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

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Citations in the corpus

Advances in Protein Chemistry and Structural Biology (2010, background): “Several early studies showed that reliable functional assignment will require sequence identity of 60–70% between the protein of unknown function and a well‐studied protein (Rost, 2002; Tian and Skolnick, 2003).”
Annotation Error in Public Databases: Misannotation of Molecular Function in Enzyme Superfamilies (2009, background): “Based on related observations, this suggestion has been previously made [54].”
Predicting protein function from sequence and structure (2007, background): “Various analyses have suggested that for functional transferability, 40% pairwise sequence identity can be used as a confident threshold to transfer the first three digits of an EC number, but to transfer all four digits of an EC number with at least 90% accuracy, >60% sequence identity is neede”
GoFDR: A sequence alignment based method for predicting protein functions. (2016, neutral): “In theory, the functional domains/residues-based approaches should be more accurate than sequence similarity based methods, because the function of a protein is often determined by a functional domain or even a small number of functionally important residues rather than by the entire sequence [33].”
KAAS: an automatic genome annotation and pathway reconstruction server (2007, background): “In previous works, the relationship between the functional conservation and the sequence similarity score was studied, and it was suggested for enzymes that from 40 to 70% sequence identity is necessary for functional prediction with 90% accuracy (5, 6 ).”