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Phylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins

Multicopper blue proteins, composed of several repetitive copper-binding domains similar to one-domain cupredoxin-like proteins, were found in almost all organisms. They are classified into the three different groups, based on their two-, three- or six-domain organization. We found orthologs of chor...

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Detalles Bibliográficos
Autores principales: Vasin, Andrey, Klotchenko, Sergey, Puchkova, Ludmila
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3600357/
https://www.ncbi.nlm.nih.gov/pubmed/23516668
http://dx.doi.org/10.1371/currents.tol.574bcb0f133fe52835911abc4e296141
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author Vasin, Andrey
Klotchenko, Sergey
Puchkova, Ludmila
author_facet Vasin, Andrey
Klotchenko, Sergey
Puchkova, Ludmila
author_sort Vasin, Andrey
collection PubMed
description Multicopper blue proteins, composed of several repetitive copper-binding domains similar to one-domain cupredoxin-like proteins, were found in almost all organisms. They are classified into the three different groups, based on their two-, three- or six-domain organization. We found orthologs of chordate six-domain copper-binding proteins in animals, plants, bacteria and archea. The phylogenetic analysis of 183 multicopper blue proteins and their copper-binding sites comparison make us think that all the modern six-domain blue proteins have originated from the common ancestral six-domain protein in the process of gene duplication and copper-binding sites loss as a result of amino acid substitutions.
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spelling pubmed-36003572013-03-19 Phylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins Vasin, Andrey Klotchenko, Sergey Puchkova, Ludmila PLoS Curr Phylogenies Multicopper blue proteins, composed of several repetitive copper-binding domains similar to one-domain cupredoxin-like proteins, were found in almost all organisms. They are classified into the three different groups, based on their two-, three- or six-domain organization. We found orthologs of chordate six-domain copper-binding proteins in animals, plants, bacteria and archea. The phylogenetic analysis of 183 multicopper blue proteins and their copper-binding sites comparison make us think that all the modern six-domain blue proteins have originated from the common ancestral six-domain protein in the process of gene duplication and copper-binding sites loss as a result of amino acid substitutions. Public Library of Science 2013-03-13 /pmc/articles/PMC3600357/ /pubmed/23516668 http://dx.doi.org/10.1371/currents.tol.574bcb0f133fe52835911abc4e296141 Text en http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Phylogenies
Vasin, Andrey
Klotchenko, Sergey
Puchkova, Ludmila
Phylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins
title Phylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins
title_full Phylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins
title_fullStr Phylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins
title_full_unstemmed Phylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins
title_short Phylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins
title_sort phylogenetic analysis of six-domain multi-copper blue proteins
topic Phylogenies
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3600357/
https://www.ncbi.nlm.nih.gov/pubmed/23516668
http://dx.doi.org/10.1371/currents.tol.574bcb0f133fe52835911abc4e296141
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