Difference between revisions of "PolX"

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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P94544 P94544]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P94544 P94544]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU28590]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU28590]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.7.7 2.7.7.7]
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.7.7 2.7.7.7]

Revision as of 09:24, 25 June 2009

  • Description: DNA polymerase X, involved in DNA repair

Gene name polX
Synonyms yshC
Essential no
Product DNA polymerase X
Function DNA repair
MW, pI 63 kDa, 5.308
Gene length, protein length 1710 bp, 570 aa
Immediate neighbours mutSB, yshB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YshC context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU28590

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1) (according to Swiss-Prot) template-dependent DNA polymerase, fills single nucleotide gaps PubMed, has intrinsic 3'-5' exonuclease activity for resecting unannealed 3'-termini in gapped DNA substrates PubMed
  • Protein family: DNA polymerase X family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions: monomeric PubMed
  • Localization:

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Margarita Salas, Madrid, Spain link

Your additional remarks

References

Benito Baños, José M Lázaro, Laurentino Villar, Margarita Salas, Miguel de Vega
Characterization of a Bacillus subtilis 64-kDa DNA polymerase X potentially involved in DNA repair.
J Mol Biol: 2008, 384(5);1019-28
[PubMed:18938175] [WorldCat.org] [DOI] (I p)

Benito Baños, José M Lázaro, Laurentino Villar, Margarita Salas, Miguel de Vega
Editing of misaligned 3'-termini by an intrinsic 3'-5' exonuclease activity residing in the PHP domain of a family X DNA polymerase.
Nucleic Acids Res: 2008, 36(18);5736-49
[PubMed:18776221] [WorldCat.org] [DOI] (I p)