It is likely the low sequence homology rendered the homology model inaccurate.
These findings, along with previous work that successfully generated a homology model with proteins of similar modest sequence identity (Misura et al. 2006), indicate that a reasonably accurate structural homology model for glp-4 VARS-2 can be generated using valRS as a template.
Importantly, previous studies have established that due to rapid evolutionary divergence of kinetochore proteins the level of sequence homology across eukaryotic species is relatively modest (between 15% 30%) with the highest levels of divergence found within Drosophila kinetochore proteins [21].
Although their putative ternary structure is well preserved (i.e. pentaspan membrane topology), their overall sequence homology determined by pairwise comparisons with human prominin-1 is rather modest with ≈70 and 45% amino acid similarity and identity, respectively (Table S4).
Fig. 1 Sequence homology analysis of BVMOLepto.
The amino acid sequence showed sequence homology with vertebrate ferritin.
Homology comparison with Actin gene sequences of other plants in the GenBank showed that it shared over 82% nucleotide sequence homology and 90% amino acid sequence homology.
The purpose of alignment is to best determine sequence homology.
Considerable sequence homology exists across different mammalian species.
No sequence homology is detectable with known proteins.
