Sequence logos of the highly conserved signal peptide and acidic propiece region for each species, based on aligned cluster sequences. Standard amino-acid symbols are used, with dark font representing more acidic residues. The predicted cleavage site is C-terminal of the conserved cysteine residue. Position 24 of the P. regilla alignment is blank because the majority of sequences had a gap at this alignment position
<p>The sequence logo representation of the frequency of the amino acid residues surrounding the oxid...
<p>Selected peptide sequences from the NC99 HA were aligned to the respective sequences from histori...
<p><b>(A)</b> The predicted full length of the peptide is 83 a.a, the underlined region is the signa...
Sequence logos of the highly conserved signal peptide and acidic propiece region for each species, b...
Signal peptide region indicated in red, predicted AMP region indicated in green and other peptides s...
<p>The conserved amino acid motifs surrounding the active site residues (boxed) are shown as logos a...
<p>(A): Alignment of amino acid sequences of the candidate OBPs. (B): Alignment of amino acid sequen...
<p>Two motifs (I-helix, and heme loop) are represented in an aligned format to show conservation acr...
<p>Dashes were introduced to improve alignment. Orange boxes indicate the last residue of the predic...
<p>Peptides are predicted based on sequence homology to previously identified peptides (both highlig...
<p>The six conserved cysteine residues were marked by dark gray. “*” indicated that all residues in ...
<p>The six conserved cysteine residues were marked by dark gray. “*” indicated that all residues in ...
<p>SNPs used in this study were conserved among species. Arrow heads indicate SNP regions of human D...
<p>Conserved residues were highlighted in gray and conserved cysteines were marked with “*” below th...
<p>Consensus sequence alignments show those amino acids conserved as a hydrophobic as α (A, V, L, I,...
<p>The sequence logo representation of the frequency of the amino acid residues surrounding the oxid...
<p>Selected peptide sequences from the NC99 HA were aligned to the respective sequences from histori...
<p><b>(A)</b> The predicted full length of the peptide is 83 a.a, the underlined region is the signa...
Sequence logos of the highly conserved signal peptide and acidic propiece region for each species, b...
Signal peptide region indicated in red, predicted AMP region indicated in green and other peptides s...
<p>The conserved amino acid motifs surrounding the active site residues (boxed) are shown as logos a...
<p>(A): Alignment of amino acid sequences of the candidate OBPs. (B): Alignment of amino acid sequen...
<p>Two motifs (I-helix, and heme loop) are represented in an aligned format to show conservation acr...
<p>Dashes were introduced to improve alignment. Orange boxes indicate the last residue of the predic...
<p>Peptides are predicted based on sequence homology to previously identified peptides (both highlig...
<p>The six conserved cysteine residues were marked by dark gray. “*” indicated that all residues in ...
<p>The six conserved cysteine residues were marked by dark gray. “*” indicated that all residues in ...
<p>SNPs used in this study were conserved among species. Arrow heads indicate SNP regions of human D...
<p>Conserved residues were highlighted in gray and conserved cysteines were marked with “*” below th...
<p>Consensus sequence alignments show those amino acids conserved as a hydrophobic as α (A, V, L, I,...
<p>The sequence logo representation of the frequency of the amino acid residues surrounding the oxid...
<p>Selected peptide sequences from the NC99 HA were aligned to the respective sequences from histori...
<p><b>(A)</b> The predicted full length of the peptide is 83 a.a, the underlined region is the signa...
DOI
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