The zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions in order to stabilize the fold. Zinc finger proteins are classified into several structural families. These families are defined by the three-dimensional structure as well as by the primary structure of the protein and the identity of the ligands coordinating the zinc ion. The vast majority typically function as interaction modules that bind DNA, RNA, proteins, or small molecules. The RING (Really Interesting New Gene) finger domain is a zinc finger which contains a Cys3HisCys4 motif that binds two zinc ions. Many proteins containing a RING finger play a key role in the ubiquitination pathway .
Tri a 41, a mitochondrial ubiquitin ligase activator of NFκB, was identified as a minor wheat allergen.
Family-defining Pfam domains (at least one of these domains is present in each family member):
|Pfam domain||Pfam clan|
|PF13920||Zinc finger, C3HC4 type (RING finger)||CL0229||Ring-finger/U-box superfamily|
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