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ACT52034.1 ACT52034.1 ACT49251.1 ACT49251.1 dnaX dnaX ACT50994.1 ACT50994.1 ACT49820.1 ACT49820.1 ACT51542.1 ACT51542.1 ACT50625.1 ACT50625.1 uvrB uvrB ACT49489.1 ACT49489.1 dnaQ dnaQ mutM mutM
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
ACT52034.1KEGG: mfa:Mfla_1553 DNA polymerase III, epsilon subunit; TIGRFAM: DNA polymerase III, epsilon subunit; PFAM: Exonuclease RNase T and DNA polymerase III; Excinuclease ABC C subunit domain protein; SMART: Exonuclease; Excinuclease ABC C subunit domain protein. (470 aa)    
Predicted Functional Partners:
ACT49251.1
DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]
  
 0.979
dnaX
DNA polymerase III, subunits gamma and tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
 
 0.978
ACT50994.1
KEGG: mfa:Mfla_1247 DNA polymerase III, alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein.
   
 0.978
ACT49820.1
KEGG: mfa:Mfla_2157 DNA polymerase III, delta subunit; TIGRFAM: DNA polymerase III, delta subunit; PFAM: DNA polymerase III delta.
   
 0.965
ACT51542.1
SMART: helicase c2; KEGG: mfa:Mfla_0411 helicase C2.
    
 0.947
ACT50625.1
TIGRFAM: DNA polymerase III, delta prime subunit; KEGG: mfa:Mfla_1499 DNA polymerase III, delta prime subunit.
  
 0.941
uvrB
Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...]
 
 
 0.930
ACT49489.1
PFAM: DNA polymerase III chi subunit HolC; KEGG: mfa:Mfla_0223 DNA polymerase III, chi subunit.
   
 0.929
dnaQ
DNA polymerase III, epsilon subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease.
  
  
0.909
mutM
formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
  
  
 0.864
Your Current Organism:
Methylovorus glucosetrophus
NCBI taxonomy Id: 582744
Other names: M. glucosetrophus SIP3-4, Methylovorus glucosetrophus SIP3-4, Methylovorus glucosetrophus str. SIP3-4, Methylovorus glucosetrophus strain SIP3-4, Methylovorus sp. SIP3-4
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