Protein Domain : Rusticyanin IPR001243

Type	Family
Description	Rusticyanin is a blue copper protein, described in an obligate acidophilic chemolithoautroph, Acidithiobacillus ferrooxidans, as an electron transfer protein. It can constitute up to 5 percent of protein in cells grown on Fe(II) and is thought to be part of an electron chain for Fe(II) oxidation, with two c-type cytochromes, an aa3-type cytochrome oxidase, and 02 as terminal electron acceptor [ , ]. It is rather closely related to sulfocyanin (). The NMR structure indicates the fold to be a compact β-barrel or β-sandwich, which contains a hydrophobic core rich in aromatic residues [ ]. Its sequence is highly diverged from related copper-blue proteins, but it has a similar active site, containing conserved His and Cys residues responsible for bindingcopper.
Short Name	Rusticyanin