The domain within your query sequence starts at position 702 and ends at position 728; the E-value for the ZnF_Rad18 domain shown below is 2.31e-8.



Rad18-like CCHC zinc finger
SMART accession number:SM00734
Description: Yeast Rad18p functions with Rad5p in error-free post-replicative DNA repair. This zinc finger is likely to bind nucleic-acids.
Interpro abstract (IPR006642):

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 a zinc finger motif found in proteins such as RAD18. The domain is a potential zinc finger for nucleic acid binding and a putative nucleotide binding sequence [(PUBMED:2970061)]. Human RAD18 accumulates very rapidly and remains for a long period of time at sites of different types of DNA damage, and is required of DNA. RAD18 appears to respond to DNA damage in two distinct ways: replication-dependent and replication-independent. The RAD18-type zinc finger located in the middle of RAD18 is responsible for the replication-independent accumulation of RAD18 following DNA damage, while a second zinc finger, SAP-type, is responsible for replication-dependent accumulation [(PUBMED:16980296)].

GO process:DNA repair (GO:0006281)
GO function:DNA binding (GO:0003677)
Family alignment:
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There are 2366 ZnF_Rad18 domains in 1659 proteins in SMART's nrdb database.

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