SMRSmall MutS-related domain
|SMART accession number:||SM00463|
|Interpro abstract (IPR002625):||This family includes the Smr (Small MutS Related) proteins, and the C-terminal region of the MutS2 protein. It has been suggested that this domain interacts with the MutS1 (P23909) protein in the case of Smr proteins and with the N-terminal MutS related region of MutS2, P94545 [(PUBMED:10431172)].|
Click on the following links for more information.
- Evolution (species in which this domain is found)
Click on to expand nodes. To display all proteins with a SMR domain in a specific node, click on it.
This tree shows only several representative species. The complete taxonomic breakdown of all proteins with SMR domain is also avaliable.
Useful shortcuts: Expand all nodes or Collapse tree
Go to specific node: Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Aravind L, Walker DR, Koonin EV
- Conserved domains in DNA repair proteins and evolution of repair systems.
- Nucleic Acids Res. 1999; 27: 1223-42
- Display abstract
A detailed analysis of protein domains involved in DNA repair was performed by comparing the sequences of the repair proteins from two well-studied model organisms, the bacterium Escherichia coli and yeast Saccharomyces cerevisiae, to the entire sets of protein sequences encoded in completely sequenced genomes of bacteria, archaea and eukaryotes. Previously uncharacterized conserved domains involved in repair were identified, namely four families of nucleases and a family of eukaryotic repair proteins related to the proliferating cell nuclear antigen. In addition, a number of previously undetected occurrences of known conserved domains were detected; for example, a modified helix-hairpin-helix nucleic acid-binding domain in archaeal and eukaryotic RecA homologs. There is a limited repertoire of conserved domains, primarily ATPases and nucleases, nucleic acid-binding domains and adaptor (protein-protein interaction) domains that comprise the repair machinery in all cells, but very few of the repair proteins are represented by orthologs with conserved domain architecture across the three superkingdoms of life. Both the external environment of an organism and the internal environment of the cell, such as the chromatin superstructure in eukaryotes, seem to have a profound effect on the layout of the repair systems. Another factor that apparently has made a major contribution to the composition of the repair machinery is horizontal gene transfer, particularly the invasion of eukaryotic genomes by organellar genes, but also a number of likely transfer events between bacteria and archaea. Several additional general trends in the evolution of repair proteins were noticed; in particular, multiple, independent fusions of helicase and nuclease domains, and independent inactivation of enzymatic domains that apparently retain adaptor or regulatory functions.
- Moreira D, Philippe H
- Smr: a bacterial and eukaryotic homologue of the C-terminal region of the MutS2 family.
- Trends Biochem Sci. 1999; 24: 298-300
- Eisen JA
- A phylogenomic study of the MutS family of proteins.
- Nucleic Acids Res. 1998; 26: 4291-300
- Display abstract
The MutS protein of Escherichia coli plays a key role in the recognition and repair of errors made during the replication of DNA. Homologs of MutS have been found in many species including eukaryotes, Archaea and other bacteria, and together these proteins have been grouped into the MutS family. Although many of these proteins have similar activities to the E.coli MutS, there is significant diversity of function among the MutS family members. This diversity is even seen within species; many species encode multiple MutS homologs with distinct functions. To better characterize the MutS protein family, I have used a combination of phylogenetic reconstructions and analysis of complete genome sequences. This phylogenomic analysis is used to infer the evolutionary relationships among the MutS family members and to divide the family into subfamilies of orthologs. Analysis of the distribution of these orthologs in particular species and examination of the relationships within and between subfamilies is used to identify likely evolutionary events (e.g. gene duplications, lateral transfer and gene loss) in the history of the MutS family. In particular, evidence is presented that a gene duplication early in the evolution of life resulted in two main MutS lineages, one including proteins known to function in mismatch repair and the other including proteins known to function in chromosome segregation and crossing-over. The inferred evolutionary history of the MutS family is used to make predictions about some of the uncharacterized genes and species included in the analysis. For example, since function is generally conserved within subfamilies and lineages, it is proposed that the function of uncharacterized proteins can be predicted by their position in the MutS family tree. The uses of phylogenomic approaches to the study of genes and genomes are discussed.
- Zhulin IB, Taylor BL, Dixon R
- PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox.
- Trends Biochem Sci. 1997; 22: 331-3
- Structure (3D structures containing this domain)
3D Structures of SMR domains in PDB
PDB code Main view Title 2d9i Solution structure of the smr domain of nedd4-binding protein 2 2vkc Solution structure of the b3bp smr domain 2zqe Crystal structure of the smr domain of thermus thermophilus muts2
- Links (links to other resources describing this domain)