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Protein Domain : IPR019786

Name  Zinc finger, PHD-type, conserved site Short Name  Zinc_finger_PHD-type_CS
Type  Conserved_site Description  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 [, , , , ]. 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 genetranscription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents the PHD (homeodomain) zinc finger domain [,], which is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in chromatin-mediated transcriptional regulation. The PHD finger motif is reminiscent of, but distinct from the C3HC4 type RING finger.The function of this domain is not yet known but in analogy with the LIM domain it could be involved in protein-protein interaction and be important for the assembly or activity of multicomponent complexes involved in transcriptional activation or repression. Alternatively, the interactions could be intra-molecular and be important in maintaining the structural integrity of the protein. In similarity to the RING finger and the LIM domain, the PHD finger is thought to bind two zinc ions.The signature of this entry starts at the first cysteine of the zinc finger region and ends at the last one. The spacing between cysteines in the PHD finger is closely related to that in the RING finger. Discrimination between these two domains with either a pattern or a profile is therefore difficult, and some rare domains are recognised by both the RING and PHD patterns and profiles. More information about these proteins can be found at Protein of the Month: Zinc Fingers [].

Publication Counts Displayer

0 Child Features

0 Contains

1 Cross References

Source . Name

Subject . Primary Identifier
PS01359 PROSITE IPR019786

2 Data Sets

Name URL
TrEMBL data set
InterPro data set  

5 Found In

DB identifier Name Short Name Type
IPR013083 Zinc finger, RING/FYVE/PHD-type Znf_RING/FYVE/PHD Domain
IPR011011 Zinc finger, FYVE/PHD-type Znf_FYVE_PHD Domain
IPR001965 Zinc finger, PHD-type Znf_PHD Domain
IPR019787 Zinc finger, PHD-finger Znf_PHD-finger Domain
IPR008087 Autoimmune regulator, AIRE AIRE Family

0 GO Annotation

0 Ontology Annotations

0 Parent Features

377 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0080265 P40798 Drosophila melanogaster
FBpp0304749 M9PDG3 Drosophila melanogaster
FBpp0304750 M9PD57 Drosophila melanogaster
FBpp0081130 Q7KSZ0 Drosophila melanogaster
FBpp0073100 Q9VZF2 Drosophila melanogaster
FBpp0074688 O97159 Drosophila melanogaster
FBpp0304462 M9PIA6 Drosophila melanogaster
FBpp0099808 Q59E34 Drosophila melanogaster
FBpp0072702 Q9W0C3 Drosophila melanogaster
FBpp0071262 Q9W352 Drosophila melanogaster
FBpp0292089 M9MS35 Drosophila melanogaster
FBpp0075510 Q9VUB5 Drosophila melanogaster
FBpp0074385 Q9VWS0 Drosophila melanogaster
FBpp0081129 Q9VI63 Drosophila melanogaster
FBpp0082081 Q9VGA4 Drosophila melanogaster
FBpp0072431 Q7YZH1 Drosophila melanogaster
FBpp0088092 Q7JVP4 Drosophila melanogaster
FBpp0072421 Q9W0T1 Drosophila melanogaster
FBpp0082953 Q9VEF5 Drosophila melanogaster
FBpp0083320 Q9VDK5 Drosophila melanogaster
FBpp0305358 Q7KV33 Drosophila melanogaster
FBpp0070864 Q9W410 Drosophila melanogaster
FBpp0084040 Q94545 Drosophila melanogaster
FBpp0080103 Q9VJY8 Drosophila melanogaster
FBpp0080104 Q8IP71 Drosophila melanogaster
FBpp0085167 Q9V9W8 Drosophila melanogaster
FBpp0074766 O16102 Drosophila melanogaster
FBpp0086102 A1ZAV3 Drosophila melanogaster
FBpp0070456 Q9W4W7 Drosophila melanogaster
FBpp0071263 Q8T3Y1 Drosophila melanogaster