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MSA of HCO

Above figure shows Kalign alignment result, with red box indicating identical residues (3) and black box indicating the conserved residues via hydropathy (10). The illustration shows that although the structural conformation of the four proteins are significantly homologous, there is a low conservation of the sequence between them.


Furthermore, Jalview has also been obtained to further illustrate the relationship between qNOR and NorC of cNOR. Quite a numerous number of conserved sequence are shown but only a few are of the same residue.


Above is the sequence comparison of cyt-c fold containing hydrophilic domain. Data taken from P. aeruginosa cytochrome c551, Rhodothermus merinus cytochrome c, G. stearothermophilus qNOR, P. aeruginosa cNOR and P. stutzeri cbb3 oxidase, reproduced from reference paper. Although the general fold morphology is homologous, the amino acid sequence yet again differs markedly.
  • Highlighted in cyan are helical regions
  • TM1 and alpha1-5 are labeled above based on the apha-helical regions in qNOR
  • Black and red dotted circles indicates the regions with high deviation in the alignment

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