Summary: Fungal Rad9-like Rad53-binding
Fungal Rad9-like Rad53-binding Provide feedback
In Saccharomyces cerevisiae the Rad9 a key adaptor protein in DNA damage checkpoint pathways. DNA damage induces Rad9 phosphorylation, and Rad53 specifically associates with this region of Rad9, when phosphorylated, via Rad53 PF00498 domains . This region is structurally composed of a pair of TUDOR domains .
Lancelot N, Charier G, Couprie J, Duband-Goulet I, Alpha-Bazin B, Quemeneur E, Ma E, Marsolier-Kergoat MC, Ropars V, Charbonnier JB, Miron S, Craescu CT, Callebaut I, Gilquin B, Zinn-Justin S; , Nucleic Acids Res. 2007;35:5898-5912.: The checkpoint Saccharomyces cerevisiae Rad9 protein contains a tandem tudor domain that recognizes DNA. PUBMED:17726056 EPMC:17726056
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013914
This entry represents a Rad53 binding domain (tudor domain) from yeast Rad9. In Saccharomyces cerevisiae (Baker s yeast), Rad9 is a key adaptor protein in DNA damage checkpoint pathways. DNA damage induces Rad9 phosphorylation and promotes the interaction between Rad9 and phosphorylated Rad53 [PUBMED:9755168]. This interaction is achieved through the Rad53 binding domain from Rad9 and the FHA domains from Rad53 (INTERPRO) [PUBMED:10518219]. Confusingly, there is another Rad9 protein found in fission yeast and other eukaryotes (which is known as Ddc1 in budding yeast) that is also involved in DNA repair. However, these proteins are not related to the Rad9 proteins covered by this entry.
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This clan covers the Tudor domain 'royal family' . This includes chromo, MBT, PWWP and tudor domains. The chromo domain is a comprised of approximately 50 amino acid residues. There are usually one to three Chromo domains found in a single protein. In some chromo domain containing proteins, a second related chromo domain has been found and is referred to as the Chromo-shadow domain. The structure of the Chromo and Chromo-shadow domains reveal an OB-fold, a fold found in a variety of prokaryotic and eukaryotic nucleic acid binding proteins. More specifically,the chromo-domain structure reveals a three beta strands that are packed against an alpha helix. Interestingly, a similar structure is found in the archaeal chromatin proteins (7kDa DNA-binding domain). These are sequence neutral DNA binding proteins. The DNA binding in these archaeal proteins is mediated through the triple stranded beta sheet. These archaeal domains are though to represent an ancestral chromo domain. Homologs of the chromo domain have been found in fission yeast, ciliated protozoa and all animal species, but appear to be absent in eubacteria, budding yeast and plants . The precise function of the chromo domain is unclear, but the chromo domain is thought to act as a targeting module for chromosomal proteins, although the chromosomal contexts and functional contexts being targeted vary. In all cases studies, the chromo domains are found in proteins that are involved in transcription regulation, positive and negative .
The clan contains the following 15 members:53-BP1_Tudor 7kD_DNA_binding Agenet Chromo Chromo_shadow DUF1325 DUF4537 MBT PWWP Rad9_Rad53_bind RBB1NT SMN TTD TUDOR Tudor-knot
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Curation and family details
|Author:||Wood V, Finn RD|
|Number in seed:||8|
|Number in full:||139|
|Average length of the domain:||136.60 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||10.65 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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