The domain within your query sequence starts at position 62 and ends at position 170; the E-value for the Mre11_DNA_bind domain shown below is 1.81e-32.
The Mre11 complex is a multi-subunit nuclease that is composed of Mre11, Rad50 and Nbs1/Xrs2, and is involved in checkpoint signalling and DNA replication (PMID:11988766). Mre11 has an intrinsic DNA-binding activity that is stimulated by Rad50 on its own or in combination with Nbs1 (PMID:10823903).
The Mre11 complex is a multi-subunit nuclease that is composed of Mre11, Rad50 and Nbs1/Xrs2, and is involved in checkpoint signalling and DNA replication [ (PUBMED:11988766) ]. Mre11 has an intrinsic DNA-binding activity that is stimulated by Rad50 on its own or in combination with Nbs1 [ (PUBMED:10823903) ].
There are 1809 Mre11_DNA_bind domains in 1809 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Mre11_DNA_bind domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Mre11_DNA_bind domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Mre11_DNA_bind domain in the selected taxonomic class.
A mechanistic basis for Mre11-directed DNA joining at microhomologies.
Proc Natl Acad Sci U S A. 2000; 97: 6409-14
Display abstract
Repair of DNA double-strand breaks in vertebrate cells occurs mainly by anend-joining process that often generates junctions with sequence homologies of a few nucleotides. Mre11 is critical for this mode of repair in budding yeast andhas been implicated in the microhomology-based joining. Here, we show that Mre11 exonuclease activity is sensitive to the presence of heterologous DNA, and to thestructure and sequence of its ends. Addition of mismatched DNA ends stimulatesdegradation of DNA by Mre11, whereas cohesive ends strongly inhibit it.Furthermore, if a sequence identity is revealed during the course of degradation,it causes Mre11 nuclease activity to pause, thus stabilizing the junction at asite of microhomology. A nuclease-deficient Mre11 mutant that still binds DNA canalso stimulate degradation by wild-type Mre11, suggesting that Mre11-DNAcomplexes may interact to bridge DNA ends and facilitate DNA joining.
