Description

IPR010666 is a Zinc finger, GRF-type.

<p>This entry represents Glycine-arginine-phenylalanine (GRF)-type zinc fingers (GRF-ZFs), 45- to 50-residue domains with a conserved GRxF motif. GRF-ZFs are widely distributed throughout eukaryotes in proteins that are involved in DNA damage response (DDR), transcriptional regulation, and RNA metabolism. GRF-ZFs are nucleic acid interaction modules and in several cases these motifs have been shown to enhance enzymatic activity. Some members of this group of proteins are rRNA N6-adenosine-methyltransferase ZCCHC4, a 28S rRNA-specific N6-adenosine-methyltransferase; DNA-(apurinic or apyrimidinic site) endonuclease 2 (APE2, known as Apn2 in yeast); DNA topoisomerase 3 and Transcription termination factor 2 [[cite:PUB00103782], [cite:PUB00103784], [cite:PUB00103785], [cite:PUB00103783]].</p> <p>This domain comprises a three-stranded anti-parallel β-sheet that folds into a crescent-shaped claw-like structure ([pdbe:5U6Z]). A single bound Zn(2+) ion plays a central structural role in this domain, and is coordinated with tetrahedral geometry by a "CHCC" sequence motif [[cite:PUB00103782], [cite:PUB00103784], [cite:PUB00103785], [cite:PUB00103783]].</p> <p>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 [[cite:PUB00035807], [cite:PUB00035805], [cite:PUB00035806], [cite:PUB00035804], [cite:PUB00014077]]. 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 [[cite:PUB00035812]]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 45

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: