|SMART accession number:||SM00412|
|Description:||binds DNA only in present of copper or silver|
|Interpro abstract (IPR001083):|
Some fungal transcription factors contain an N-terminal domain, the copper fist, which seems to be involved in copper-dependent DNA-binding [(PUBMED:8262047), (PUBMED:8509391)]. These proteins activate the transcription of the metallothionein gene in response to copper. Metallothionein maintains copper levels in yeast [(PUBMED:3052856), (PUBMED:8262047)]. The copper fist domain, which is similar in structure to metallothionein itself, undergoes a large conformational change on copper-binding that allows DNA-binding. The domain contains a conserved array of zinc-binding residues (Cys-X2-Cys-X8-Cys-X-His) and forms a three-stranded antiparallel beta-sheet with two short helical segments that project from one end of the beta-sheet [(PUBMED:9665167)]. Conserved residues form a basic patch that may be important for DNA binding.
|GO process:||regulation of transcription, DNA-templated (GO:0006355)|
|GO component:||nucleus (GO:0005634)|
|GO function:||copper ion binding (GO:0005507), DNA binding (GO:0003677), sequence-specific DNA binding transcription factor activity (GO:0003700)|
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- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Literature (relevant references for this domain)
- Structure (3D structures containing this domain)
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