Protein Family Models

This is N-terminal domain containing a mononuclear metal center for zinc binding found in copper chaperone CopZ proteins [1]. [1]. 17609202. Characterization and structure of a Zn2+ and [2Fe-2S]-containing. copper chaperone from Archaeoglobus fulgidus.. Sazinsky MH, LeMoine B, Orofino M, Davydov R, Bencze KZ,. Stemmler TL, Hoffman BM, Arguello JM, Rosenzweig AC;. J Biol Chem. 2007;282:25950-25959. (from Pfam)

Date:

2024-08-14

Members of this family, including Csac_0668 from Caldicellulosiruptor saccharolyticus, are homologous to the N-terminal half of the copper chaperone CopZ from Archaeoglobus fulgidus. While the C-terminal half of CopZ resembles other previously known copper-binding domain, and binds a copper atom, the N-terminus was found to bind an additional copper and a 2Fe-2S iron-sulfur cluster. Members of the family described here contain an additional 20 amino acids N-terminal to region that aligns to CopZ, containing multiple Cys residues (sometimes four in a row) or selenocysteine in a suggested metal-binding CU motif. The proposed function for members of this family is as a metallochaperone. Note that some homologs outside the scope of this family, such as WP_240162626.1, similarly are selenoproteins but have the selenocysteine at different site.

Date:

2024-04-11