From the point of view of sequence or structure alignment, this would mean that the charged residues are not conserved, yet they are still presented in both interfaces.
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Although the DNA sequences from strains were more conserved, we still detected significant differences between isolates: these four strains shared 98.4 100% amino acid identity.
The N gene was highly conserved but still had some unique point mutations as well as conserved regions.
Although p.Gln609Glu is less conserved, we still believe that Glutamine to Glutamic acid substitution may have an effect on protein conformation as two adjacent acidic amino acids will be formed as the result of the substitution.
The regulatory pathways in which these genes are involved show us that these genes are all related to some part of Drosophila embryo development, some of them with highly conserved functions still observed in the preimplantation pathway described.
De novo Fe-S cluster biogenesis is a highly conserved but still poorly characterized process that occurs in mitochondria in eukaryotes [see review from Lill (Lill, 2009) and commentary from Rouault in this issue of Disease Models & Mechanisms (Rouault, 2012)].
The sequence of the latter was poorly conserved but still presents characteristics of a cystine-knot protein and contains a potential glycosylation site in a conserved position with other TSHβ subunits (Additional file 1: GPHβ subunit sequences) suggesting that it must be able to form a heterodimer with an α subunit and play a physiological role.
For instance, miRNAs that were poorly conserved could still be highly expressed, as was observed with miR-2478 (a bovine specific miRNA) which was non-clustered and poorly conserved, but the most highly expressed miRNA in bovine adipose tissue (Additional file 1).
