<p>The death domain (first domain), two conserved repeat motifs (two middle sequences), and kinase domain (last domain) are shadowed orderly. The stop codon is indicated by an asterisk (*). GD dipeptide rather than RD dipeptide is shown in blue frame.</p
Sequence logos of the highly conserved signal peptide and acidic propiece region for each species, b...
<p>The signal peptide (SP) is a sequence potentially recognized by the sec machinery and cleaved dur...
<p>Amino acid sequence identity and similarity of the relatively conserved regions (brown bars in <a...
<p>The death domain (the first domain) and kinase domain (the second domain) are shadowed. The stop ...
<p>Numbering indicates the position of the first and last residue in each aligned sequence. Proteins...
<p>The putative signal peptide is boxed, while the mature peptide is indicated in bold type, while t...
<p>Identical or similar amino acids are shaded in black and grey, respectively. The locations of the...
<p>The stop codon is indicated with an asterisk. The putative N-terminal signal peptide is underline...
<p>The secondary structure is depicted above the primary sequence. Red arrows above the sequences co...
<p>(14 aa to 144 aa, yellow) and the crystal structure of DmTube DD (PDB ID: 1d2z, chain B) (red) (A...
<p>The amino acid numbers corresponding to DD regions for each representative sequence are shown bes...
<p>A. Sequence analysis of the cDNA and predicted peptide sequences of <i>As-caspase-1</i>. The star...
<p>Amino acids are numbered in the N-terminal extracellular domain (NECD) according to the numbering...
The initiation and stop codons are marked with boxes. The α-crystallin domain (ACD) is shaded in lig...
The identification of many homologs and paralogs of the most famous tumor suppressor, p53, has expan...
Sequence logos of the highly conserved signal peptide and acidic propiece region for each species, b...
<p>The signal peptide (SP) is a sequence potentially recognized by the sec machinery and cleaved dur...
<p>Amino acid sequence identity and similarity of the relatively conserved regions (brown bars in <a...
<p>The death domain (the first domain) and kinase domain (the second domain) are shadowed. The stop ...
<p>Numbering indicates the position of the first and last residue in each aligned sequence. Proteins...
<p>The putative signal peptide is boxed, while the mature peptide is indicated in bold type, while t...
<p>Identical or similar amino acids are shaded in black and grey, respectively. The locations of the...
<p>The stop codon is indicated with an asterisk. The putative N-terminal signal peptide is underline...
<p>The secondary structure is depicted above the primary sequence. Red arrows above the sequences co...
<p>(14 aa to 144 aa, yellow) and the crystal structure of DmTube DD (PDB ID: 1d2z, chain B) (red) (A...
<p>The amino acid numbers corresponding to DD regions for each representative sequence are shown bes...
<p>A. Sequence analysis of the cDNA and predicted peptide sequences of <i>As-caspase-1</i>. The star...
<p>Amino acids are numbered in the N-terminal extracellular domain (NECD) according to the numbering...
The initiation and stop codons are marked with boxes. The α-crystallin domain (ACD) is shaded in lig...
The identification of many homologs and paralogs of the most famous tumor suppressor, p53, has expan...
Sequence logos of the highly conserved signal peptide and acidic propiece region for each species, b...
<p>The signal peptide (SP) is a sequence potentially recognized by the sec machinery and cleaved dur...
<p>Amino acid sequence identity and similarity of the relatively conserved regions (brown bars in <a...