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Phylogenetic analysis of six-domain multi-copper blue proteins.

ABSTRACT: 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.

SUBMITTER: Vasin A

PROVIDER: S-EPMC3600357 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Phylogenetic analysis of six-domain multi-copper blue proteins.

Vasin Andrey A Klotchenko Sergey S Puchkova Ludmila L

PLoS currents 20130313

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 ...[more]

PMID: 23516668

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