Summary: His(2)-Cys(2) zinc finger
His(2)-Cys(2) zinc finger Provide feedback
This domain binds to histone upstream activating sequence (UAS) elements that are found in histone gene promoters .
Mendiratta G, Eriksson PR, Shen CH, Clark DJ; , J Biol Chem. 2006;281:7040-7048.: The DNA-binding domain of the yeast Spt10p activator includes a zinc finger that is homologous to foamy virus integrase. PUBMED:16415340 EPMC:16415340
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015416
Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [PUBMED:10529348, PUBMED:15963892, PUBMED:15718139, PUBMED:17210253, PUBMED:12665246]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [PUBMED:11179890]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
This entry represents an H2C2-type zinc finger that binds to histone upstream activating sequence (UAS) elements found in histone gene promoters [PUBMED:16415340].
More information about these proteins can be found at Protein of the Month: Zinc Fingers [PUBMED:].
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a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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Curation and family details
|Author:||Mistry J, Wood V|
|Number in seed:||11|
|Number in full:||664|
|Average length of the domain:||39.20 aa|
|Average identity of full alignment:||51 %|
|Average coverage of the sequence by the domain:||10.82 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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