z-logo
open-access-imgOpen Access
Phylogenetic Analysis of Six-Domain Multi-Copper Blue Proteins
Author(s) -
Andrey V. Vasin,
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom