In fact, in all four UPF0201 proteins examined residues predicted to be involved in RNA binding are not conserved.
It has been demonstrated that the amino acid residues involved in DNA binding are not conserved between AP2 and ERFs [ 11, 12].
The N-terminal Ig like domains of ROBO1 and ROBO4 are 42% identical but the residues identified for SLIT2 binding are not conserved in ROBO4 and are replaced by residues that are not compatible with binding of SLIT2.
Sequence alignments with homologues and structural comparisons with CysK, a cysteine synthase that does not utilize a sulfur carrier protein, revealed high conservation of active site residues; however, residues in CysM responsible for CysO binding are not conserved.
In addition, molecular models based on the 3D structures of the HRM of B1/secretin-like GPCR of the GLP receptor group show that features crucial for ligand binding are not conserved in aGPCR, although hormone binding to secretin-type HRM might differ.
Nevertheless, the identification of numerous species-specific responses, evidence of divergent gene expression responses between species, and the discovery of distinct putative primary response sets in each cell line provides further compelling evidence that the effects of TCDD post-AhR binding are not conserved between species.
Curiously, the cell invasion binding site was not conserved in T. parva and B. bovis.
The terminal sequence of the K. setae chromosome was distinct from any of these groups; while the first 13 bp sequence exactly matched with that of major Streptomyces groups I and II (Supplementary Fig. S1), the subsequent region containing palindrome structures and loops, which are known in Streptomyces to be required for binding of telomere-associated protein (Tap), was not conserved.
Some positively charged or polar residues that have been previously identified as critical for lipid binding in this ligand-binding triangle are not conserved in APPL1 (Supplementary Figures 1 and 3), consistent with the fact that APPL1 alone lacks membrane binding ability.
The metal binding residues are not conserved.
