Difference between revisions of "PolX"
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| − | [[Margarita Salas]], Madrid, Spain | + | [[Margarita Salas]], Madrid, Spain [http://www.cbm.uam.es/mkfactory.esdomain/webs/CBMSO/plt_LineasInvestigacion.aspx?IdObjeto=28 link] |
=Your additional remarks= | =Your additional remarks= | ||
Revision as of 14:57, 30 January 2009
- Description: DNA polymerase X, involved in DNA repair
| Gene name | polX |
| Synonyms | yshC |
| Essential | |
| Product | DNA polymerase X |
| Function | involved in base excision repair |
| MW, pI | 63 kDa, 5.308 |
| Gene length, protein length | 1710 bp, 570 aa |
| Immediate neighbours | |
| Gene sequence (+200bp) | Protein sequence |
Genetic context 
| |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 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:
- Swiss prot entry:
- KEGG entry:
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
- Banos et al. (2008) Characterization of a Bacillus subtilis 64 kDa DNA polymerase X potentially involved in DNA repair. J. Mol. Biol. 384: 1019-1028. PubMed
- Banos et al. (2008) Editing of misaligned 3'-termini by an intrinsic 3'-5' exonuclease activity residing in the PHP domain of a family X DNA polymerase. Nucl. Acids Res. 36: 5736-5749. PubMed
