alignx application (vector nti advance™ 11 package Search Results


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Alignment of Characterized AAE13 Homologs. Malonyl-CoA synthetases from Arabodopsis (AtAAE13), human (Hs ACSF3), B. japonicum (Bradyrhizobium), and Rhizobium leguminosarum (Rhizobium) were aligned using <t>Vector</t> <t>NTI.</t> Dark-gray shading indicates identical residues; light-gray shading indicates conserved substitutions. The underlined sequence is the conserved 12–amino acid AMP binding motif (PS00455).
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Alignment of Characterized AAE13 Homologs. Malonyl-CoA synthetases from Arabodopsis (AtAAE13), human (Hs ACSF3), B. japonicum (Bradyrhizobium), and Rhizobium leguminosarum (Rhizobium) were aligned using <t>Vector</t> <t>NTI.</t> Dark-gray shading indicates identical residues; light-gray shading indicates conserved substitutions. The underlined sequence is the conserved 12–amino acid AMP binding motif (PS00455).
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Alignment of Characterized AAE13 Homologs. Malonyl-CoA synthetases from Arabodopsis (AtAAE13), human (Hs ACSF3), B. japonicum (Bradyrhizobium), and Rhizobium leguminosarum (Rhizobium) were aligned using <t>Vector</t> <t>NTI.</t> Dark-gray shading indicates identical residues; light-gray shading indicates conserved substitutions. The underlined sequence is the conserved 12–amino acid AMP binding motif (PS00455).
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Alignment of Characterized AAE13 Homologs. Malonyl-CoA synthetases from Arabodopsis (AtAAE13), human (Hs ACSF3), B. japonicum (Bradyrhizobium), and Rhizobium leguminosarum (Rhizobium) were aligned using <t>Vector</t> <t>NTI.</t> Dark-gray shading indicates identical residues; light-gray shading indicates conserved substitutions. The underlined sequence is the conserved 12–amino acid AMP binding motif (PS00455).
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Alignment of Characterized AAE13 Homologs. Malonyl-CoA synthetases from Arabodopsis (AtAAE13), human (Hs ACSF3), B. japonicum (Bradyrhizobium), and Rhizobium leguminosarum (Rhizobium) were aligned using <t>Vector</t> <t>NTI.</t> Dark-gray shading indicates identical residues; light-gray shading indicates conserved substitutions. The underlined sequence is the conserved 12–amino acid AMP binding motif (PS00455).
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Alignment of Characterized AAE13 Homologs. Malonyl-CoA synthetases from Arabodopsis (AtAAE13), human (Hs ACSF3), B. japonicum (Bradyrhizobium), and Rhizobium leguminosarum (Rhizobium) were aligned using <t>Vector</t> <t>NTI.</t> Dark-gray shading indicates identical residues; light-gray shading indicates conserved substitutions. The underlined sequence is the conserved 12–amino acid AMP binding motif (PS00455).
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Alignment of Characterized AAE13 Homologs. Malonyl-CoA synthetases from Arabodopsis (AtAAE13), human (Hs ACSF3), B. japonicum (Bradyrhizobium), and Rhizobium leguminosarum (Rhizobium) were aligned using <t>Vector</t> <t>NTI.</t> Dark-gray shading indicates identical residues; light-gray shading indicates conserved substitutions. The underlined sequence is the conserved 12–amino acid AMP binding motif (PS00455).
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Alignment of the putative L1-binding domains of selected L2 proteins. Alignments were generated with the assistance of Vector <t>NTI</t> <t>AlignX</t> software (InforMax). Conserved residues are in blue. Boxed residues indicate the hydrophobic region between the conserved prolines at 413 and 419 of HPV11 L2; negatively charged residues within this region are highlighted in yellow. Asterisks indicate HPV11 L2 amino acids subjected to site-directed mutagenesis with the change indicated above each asterisk. The combined alanine- and leucine-to-glutamine changes at 417 and 418 of HPV11 L2, indicated in red, severely disrupted L1 binding. Underlined residues in the HPV5 sequence are those that are different from the National Center for Biotechnology Information (NCBI) reference sequence (Table ​(Table2).2). Amino acids included in the alignment are indicated in brackets at the right.
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Image Search Results


Alignment of Characterized AAE13 Homologs. Malonyl-CoA synthetases from Arabodopsis (AtAAE13), human (Hs ACSF3), B. japonicum (Bradyrhizobium), and Rhizobium leguminosarum (Rhizobium) were aligned using Vector NTI. Dark-gray shading indicates identical residues; light-gray shading indicates conserved substitutions. The underlined sequence is the conserved 12–amino acid AMP binding motif (PS00455).

Journal: The Plant Cell

Article Title: Malonyl-CoA Synthetase, Encoded by ACYL ACTIVATING ENZYME13 , Is Essential for Growth and Development of Arabidopsis [C] [W] [OA]

doi: 10.1105/tpc.111.086140

Figure Lengend Snippet: Alignment of Characterized AAE13 Homologs. Malonyl-CoA synthetases from Arabodopsis (AtAAE13), human (Hs ACSF3), B. japonicum (Bradyrhizobium), and Rhizobium leguminosarum (Rhizobium) were aligned using Vector NTI. Dark-gray shading indicates identical residues; light-gray shading indicates conserved substitutions. The underlined sequence is the conserved 12–amino acid AMP binding motif (PS00455).

Article Snippet: Amino acid sequences were aligned using AlignX program in Vector NTI (Informax).

Techniques: Plasmid Preparation, Sequencing, Binding Assay

Alignment of the putative L1-binding domains of selected L2 proteins. Alignments were generated with the assistance of Vector NTI AlignX software (InforMax). Conserved residues are in blue. Boxed residues indicate the hydrophobic region between the conserved prolines at 413 and 419 of HPV11 L2; negatively charged residues within this region are highlighted in yellow. Asterisks indicate HPV11 L2 amino acids subjected to site-directed mutagenesis with the change indicated above each asterisk. The combined alanine- and leucine-to-glutamine changes at 417 and 418 of HPV11 L2, indicated in red, severely disrupted L1 binding. Underlined residues in the HPV5 sequence are those that are different from the National Center for Biotechnology Information (NCBI) reference sequence (Table ​(Table2).2). Amino acids included in the alignment are indicated in brackets at the right.

Journal:

Article Title: Interactions between Papillomavirus L1 and L2 Capsid Proteins

doi: 10.1128/JVI.77.8.4818-4826.2003

Figure Lengend Snippet: Alignment of the putative L1-binding domains of selected L2 proteins. Alignments were generated with the assistance of Vector NTI AlignX software (InforMax). Conserved residues are in blue. Boxed residues indicate the hydrophobic region between the conserved prolines at 413 and 419 of HPV11 L2; negatively charged residues within this region are highlighted in yellow. Asterisks indicate HPV11 L2 amino acids subjected to site-directed mutagenesis with the change indicated above each asterisk. The combined alanine- and leucine-to-glutamine changes at 417 and 418 of HPV11 L2, indicated in red, severely disrupted L1 binding. Underlined residues in the HPV5 sequence are those that are different from the National Center for Biotechnology Information (NCBI) reference sequence (Table ​(Table2).2). Amino acids included in the alignment are indicated in brackets at the right.

Article Snippet: These full-length L2 sequences were aligned with the full-length sequence of HPV11 L2 by using Vector NTI AlignX software (InforMax) to define candidate amino acids for incorporation into each construct (Table ).

Techniques: Binding Assay, Generated, Plasmid Preparation, Software, Mutagenesis, Sequencing