Summary: impB/mucB/samB family C-terminal domain
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impB/mucB/samB family C-terminal domain Provide feedback
These proteins are involved in UV protection (Swiss).
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This tab holds annotation information from the InterPro database.
InterPro entry IPR017961
This entry represents the little finger domain found in Y-family (lesion bypass) DNA polymerases. Y-family polymerases were originally known as UmuC/DinB/Rev1/Rad30 after each branch of the family. These enzymes are characterised by their low-fidelity synthesis on undamaged DNA templates and by their ability to traverse replication-blocking lesions. By contrast, high-fidelity polymerases (such as DNA polymerase III) are sensitive to distortions in the DNA template. As a result, Y-family polymerases can extend primer strands across DNA strand lesions that would otherwise stall replicative polymerases. To minimize mutations through their low fidelity synthesis, these enzymes are regulated, and are thought to interact with processivity factors, beta-clamp or proliferating cell nuclear antigen (PCNA), which are also essential for the function of replicative DNA polymerases [PUBMED:14592985]. Organisms can contain more than one Y-family polymerase, each with a unique DNA damage bypass and fidelity profile. For example, humans posses four Y-family polymerases: DNA polymerases kappa, iota, eta and Rev1. Y-family polymerases show no homology to DNA polymerases from the A-, B-, C-, D- or X-families [PUBMED:11595188].
The Y-family of DNA polymerases includes the following enzymes:
- Prokaryotic DNA polymerase IV (DinB) [PUBMED:14592985].
- Archaeal DinB homologue DNA polymerase IV [PUBMED:11595188].
- Eukaryotic DinB homologue DNA polymerase kappa [PUBMED:15296733].
- Prokarytoic DNA repair proteins UmuC and UmuD [PUBMED:17207624].
- Eukaryotic Rad30 homologues DNA polymerase eta and iota [PUBMED:11545743, PUBMED:16819516].
- Eukaryotic DNA repair protein Rev1 [PUBMED:18603483].
Human DNA polymerase kappa is a right-handed shaped molecule with palm, fingers, thumb, little finger and wrist subdomains [PUBMED:15296733]. This entry represents the little finger domain.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||DNA-directed DNA polymerase activity (GO:0003887)|
|damaged DNA binding (GO:0003684)|
|Biological process||DNA repair (GO:0006281)|
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Curation and family details
|Seed source:||Pfam-B_1349 (release 2.1)|
|Number in seed:||106|
|Number in full:||7945|
|Average length of the domain:||123.60 aa|
|Average identity of full alignment:||19 %|
|Average coverage of the sequence by the domain:||27.86 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||3|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the IMS_C domain has been found. There are 220 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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