<p>These thioredoxin-like domains of the <i>B. distachyon</i> were annotated in Phytozome database, and comparative analysis used BioEdit software. Residues highlighted in deep blue and green show they were identical and similar, respectively. Open bars and arrowheads represent the α helices and β strands, respectively. The red box indicates the -CxxC- catalytic site, and red arrows indicate the glutamicacid–lysine charged pair. Blue and yellow arrows represent the conserved arginine (R) and the <i>cis</i> pralines (P) near the active site, respectively.</p
<p>Full-length <i>P. capsici</i> homologous sequences were translated using BioEdit. (A) Pc22053. Re...
ABSTRACT Protein structure classification is necessary to comprehend the rapidly growing struc-tural...
Protein disulfide isomerases (PDIs) catalyze the formation, breakage, and rearrangement of disulfide...
<p>A, active site containing thioredoxin-like domain; b, inactive thioredoxin-like domain (superscri...
<p>The tertiary structure was predicted by the Phyre2 server, and the abb′xa′c (five domains and one...
<p>(A) Occurrence of the domain in protein disulfide isomerases and other proteins. Human ERp57 is s...
A. Alignment of P. berghei with recently characterized PhLP-3 homologs of different species using th...
The group of proteins that contain a thioredoxin (Trx) fold is huge and diverse. Assessment of the v...
<p><b>Copyright information:</b></p><p>Taken from "A tale of two ferredoxins: sequence similarity an...
A. Schematics of PbPhLP-3 showing the predicted domains. The sequence of the thioredoxin domain is s...
<p>The black and gray boxes show the consensus residues on PCS. The black boxes indicate identical a...
The group of proteins that contain a thioredoxin (Trx) fold is huge and diverse. Assessment of the v...
<p>ClustalW alignment of PNP protein sequences from <i>T. gondii</i> (TgPNP), <i>P.yoelli</i> (PyPNP...
<p>Amino acid sequence alignment of <i>P. aeruginosa</i> and <i>B. phytofirmans</i> Tse1 (A) and Tsi...
<p>Identical residues among all MDHs were shown in black boxes. The representative conserved regions...
<p>Full-length <i>P. capsici</i> homologous sequences were translated using BioEdit. (A) Pc22053. Re...
ABSTRACT Protein structure classification is necessary to comprehend the rapidly growing struc-tural...
Protein disulfide isomerases (PDIs) catalyze the formation, breakage, and rearrangement of disulfide...
<p>A, active site containing thioredoxin-like domain; b, inactive thioredoxin-like domain (superscri...
<p>The tertiary structure was predicted by the Phyre2 server, and the abb′xa′c (five domains and one...
<p>(A) Occurrence of the domain in protein disulfide isomerases and other proteins. Human ERp57 is s...
A. Alignment of P. berghei with recently characterized PhLP-3 homologs of different species using th...
The group of proteins that contain a thioredoxin (Trx) fold is huge and diverse. Assessment of the v...
<p><b>Copyright information:</b></p><p>Taken from "A tale of two ferredoxins: sequence similarity an...
A. Schematics of PbPhLP-3 showing the predicted domains. The sequence of the thioredoxin domain is s...
<p>The black and gray boxes show the consensus residues on PCS. The black boxes indicate identical a...
The group of proteins that contain a thioredoxin (Trx) fold is huge and diverse. Assessment of the v...
<p>ClustalW alignment of PNP protein sequences from <i>T. gondii</i> (TgPNP), <i>P.yoelli</i> (PyPNP...
<p>Amino acid sequence alignment of <i>P. aeruginosa</i> and <i>B. phytofirmans</i> Tse1 (A) and Tsi...
<p>Identical residues among all MDHs were shown in black boxes. The representative conserved regions...
<p>Full-length <i>P. capsici</i> homologous sequences were translated using BioEdit. (A) Pc22053. Re...
ABSTRACT Protein structure classification is necessary to comprehend the rapidly growing struc-tural...
Protein disulfide isomerases (PDIs) catalyze the formation, breakage, and rearrangement of disulfide...