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Despite only a moderate level of sequence identity (∼36%) between Mt-KasB and E. coli FabF, the two enzymes display identical folds (Suppl. Figure 1A).
Mt-PrsA shares very high sequence identity with its Corynebacterineae counterparts (92% Mycobacterium leprae, 87% M. smegmatis and 71% C. glutamicum) and a moderate level of sequence identity with Mt-PrsA homologs in S. coleicolor (61%), E. coli (43%) and B. subtilis (43%).
Similar(58)
The fold of PfuMBP is very similar to that of the orthologous MBP from E. coli (EcoMBP), despite the moderate level of sequence identity between the two proteins (27%% identity, 46%% similarity).
An alignment of NHase, NHLP and NHLP-Burk reveals a moderate level of sequence similarity.
Sequence comparison of the PBP-βL domain of LACTB with the LPBP-B proteins indicated a moderate degree of sequence identity (16 27%).
However, slightly more than half of the 2670 sequences fall into multi-sequence contigs, indicating a moderate level of redundancy in DArT marker identity.
The VP6 nucleotide and amino acid sequences of BR59, BR60, and BR63 samples did not show high identities with VP6 sequences from RVs A, C, D, and F, but showed a moderate level of relatedness to VP6 sequences of species RVB, in agreement with previous reports (10, 12 ).
There is a moderate level of evidence that food activities play a role in the maintenance and change in many different identities.
Despite a low level of sequence identity, the three-dimensional structures determined display a nearly superimposable α/β folding pattern.
xOX2R shares a high level of sequence identity (80%) and structural similarity with its mammalian orthologs.
These two sequences display a low level of sequence identity (less than 30%), especially concentrated in the C-terminal segment.
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