Open AccessPhylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins
Author(s) -
А. В. Васин,
С. А. Клотченко,
L. V. Puchkova
Publication year - 2013
Publication title -
plos currents
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.282
H-Index - 49
ISSN - 2157-3999
DOI - 10.1371/currents.tol.574bcb0f133fe52835911abc4e296141
Subject(s) - phylogenetic tree , chordate , gene duplication , domain (mathematical analysis) , phylogenetics , copper , protein domain , gene , multicopper oxidase , binding domain , biology , amino acid , computational biology , evolutionary biology , genetics , binding site , chemistry , biochemistry , vertebrate , mathematical analysis , mathematics , organic chemistry , laccase , enzyme
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.