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clustal omega61 multiple sequence alignment  (InterPro Inc)

 
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    Structured Review

    InterPro Inc clustal omega61 multiple sequence alignment
    (A) The mature nisin peptide has thioether crosslinks between Cys and dehydroalanine (Dha) and dehydrobutyrine (Dhb) residues. (B) The sactipeptide subtilosin A is shown, highlighting the three thioether crosslinks. In its fully mature form, subtilosin A is circularized. The stereochemistry at the three attachment sites is shown in red. The sactipeptides are distinct from the lanthipeptides in that the thioether crosslinks are formed to the Cα of the peptide. (C) Sequence logo for the SCIFF peptides showing the conserved C-terminal sequence. The figure was generated by aligning 100 SCIFF sequences selected from Interpro family IPR023975 using the Clustal <t>Omega61</t> multiple sequence alignment and visualized by Weblogo.62,63
    Clustal Omega61 Multiple Sequence Alignment, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/clustal omega61 multiple sequence alignment/product/InterPro Inc
    Average 90 stars, based on 1 article reviews
    clustal omega61 multiple sequence alignment - by Bioz Stars, 2026-05
    90/100 stars

    Images

    1) Product Images from "Biochemical and spectroscopic characterization of a radical SAM enzyme involved in the formation of a peptide thioether crosslink"

    Article Title: Biochemical and spectroscopic characterization of a radical SAM enzyme involved in the formation of a peptide thioether crosslink

    Journal: Biochemistry

    doi: 10.1021/acs.biochem.6b00145

    (A) The mature nisin peptide has thioether crosslinks between Cys and dehydroalanine (Dha) and dehydrobutyrine (Dhb) residues. (B) The sactipeptide subtilosin A is shown, highlighting the three thioether crosslinks. In its fully mature form, subtilosin A is circularized. The stereochemistry at the three attachment sites is shown in red. The sactipeptides are distinct from the lanthipeptides in that the thioether crosslinks are formed to the Cα of the peptide. (C) Sequence logo for the SCIFF peptides showing the conserved C-terminal sequence. The figure was generated by aligning 100 SCIFF sequences selected from Interpro family IPR023975 using the Clustal Omega61 multiple sequence alignment and visualized by Weblogo.62,63
    Figure Legend Snippet: (A) The mature nisin peptide has thioether crosslinks between Cys and dehydroalanine (Dha) and dehydrobutyrine (Dhb) residues. (B) The sactipeptide subtilosin A is shown, highlighting the three thioether crosslinks. In its fully mature form, subtilosin A is circularized. The stereochemistry at the three attachment sites is shown in red. The sactipeptides are distinct from the lanthipeptides in that the thioether crosslinks are formed to the Cα of the peptide. (C) Sequence logo for the SCIFF peptides showing the conserved C-terminal sequence. The figure was generated by aligning 100 SCIFF sequences selected from Interpro family IPR023975 using the Clustal Omega61 multiple sequence alignment and visualized by Weblogo.62,63

    Techniques Used: Sequencing, Generated



    Similar Products

    clustal omega61 multiple sequence alignment  (InterPro Inc)
    90
    InterPro Inc clustal omega61 multiple sequence alignment
    (A) The mature nisin peptide has thioether crosslinks between Cys and dehydroalanine (Dha) and dehydrobutyrine (Dhb) residues. (B) The sactipeptide subtilosin A is shown, highlighting the three thioether crosslinks. In its fully mature form, subtilosin A is circularized. The stereochemistry at the three attachment sites is shown in red. The sactipeptides are distinct from the lanthipeptides in that the thioether crosslinks are formed to the Cα of the peptide. (C) Sequence logo for the SCIFF peptides showing the conserved C-terminal sequence. The figure was generated by aligning 100 SCIFF sequences selected from Interpro family IPR023975 using the Clustal <t>Omega61</t> multiple sequence alignment and visualized by Weblogo.62,63
    Clustal Omega61 Multiple Sequence Alignment, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/clustal omega61 multiple sequence alignment/product/InterPro Inc
    Average 90 stars, based on 1 article reviews
    clustal omega61 multiple sequence alignment - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    (A) The mature nisin peptide has thioether crosslinks between Cys and dehydroalanine (Dha) and dehydrobutyrine (Dhb) residues. (B) The sactipeptide subtilosin A is shown, highlighting the three thioether crosslinks. In its fully mature form, subtilosin A is circularized. The stereochemistry at the three attachment sites is shown in red. The sactipeptides are distinct from the lanthipeptides in that the thioether crosslinks are formed to the Cα of the peptide. (C) Sequence logo for the SCIFF peptides showing the conserved C-terminal sequence. The figure was generated by aligning 100 SCIFF sequences selected from Interpro family IPR023975 using the Clustal Omega61 multiple sequence alignment and visualized by Weblogo.62,63

    Journal: Biochemistry

    Article Title: Biochemical and spectroscopic characterization of a radical SAM enzyme involved in the formation of a peptide thioether crosslink

    doi: 10.1021/acs.biochem.6b00145

    Figure Lengend Snippet: (A) The mature nisin peptide has thioether crosslinks between Cys and dehydroalanine (Dha) and dehydrobutyrine (Dhb) residues. (B) The sactipeptide subtilosin A is shown, highlighting the three thioether crosslinks. In its fully mature form, subtilosin A is circularized. The stereochemistry at the three attachment sites is shown in red. The sactipeptides are distinct from the lanthipeptides in that the thioether crosslinks are formed to the Cα of the peptide. (C) Sequence logo for the SCIFF peptides showing the conserved C-terminal sequence. The figure was generated by aligning 100 SCIFF sequences selected from Interpro family IPR023975 using the Clustal Omega61 multiple sequence alignment and visualized by Weblogo.62,63

    Article Snippet: The figure was generated by aligning 100 SCIFF sequences selected from Interpro family IPR023975 using the Clustal Omega61 multiple sequence alignment and visualized by Weblogo.62,63.

    Techniques: Sequencing, Generated