The domain within your query sequence starts at position 1 and ends at position 61; the E-value for the Metallothio domain shown below is 2e-21.



PFAM accession number:PF00131
Interpro abstract (IPR003019):

Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ (PUBMED:1779825) (PUBMED:2959513) ]. An empirical classification into three classes has been proposed by Fowler and coworkers [ (PUBMED:2959504) ] and Kojima [ (PUBMED:1779826) ]. Members of class I are defined to include polypeptides related in the positions of their cysteines to equine MT-1B, and include mammalian MTs as well as from crustaceans and molluscs. Class II groups MTs from a variety of species, including sea urchins, fungi, insects and cyanobacteria. Class III MTs are atypical polypeptides composed of gamma-glutamylcysteinyl units [ (PUBMED:2959504) ].

This original classification system has been found to be limited, in the sense that it does not allow clear differentiation of patterns of structural similarities, either between or within classes. Subsequently, a new classification was proposed on the basis of sequence similarity derived from phylogenetic relationships, which basically proposes an MT family for each main taxonomic group of organisms [ (PUBMED:21633816) ].

This entry includes metallothioneins from vertebrates [ (PUBMED:22791193) ] and MT-10 type metallothioneins from aquatic molluscs [ (PUBMED:18389296) ].

GO function:metal ion binding (GO:0046872)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Metallothio