Nodes:
Network nodes represent proteins
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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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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gene co-occurrence
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ruvCCrossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. (158 aa)    
Predicted Functional Partners:
ruvA
Holliday junction DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
 
 0.998
ruvB
Holliday junction DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
 
 0.953
ADD67271.1
PFAM: protein of unknown function DUF28; KEGG: gsu:GSU1074 hypothetical protein.
 
  
 0.850
murB
UDP-N-acetylenolpyruvoylglucosamine reductase; Cell wall formation.
     
 0.640
ADD67318.1
KEGG: geo:Geob_3446 single-stranded-DNA-specific exonuclease RecJ; TIGRFAM: single-stranded-DNA-specific exonuclease RecJ; PFAM: phosphoesterase RecJ domain protein; phosphoesterase DHHA1.
 
 
 
 0.635
ADD69695.1
KEGG: gur:Gura_4031 Mg chelatase, subunit ChlI; TIGRFAM: Mg chelatase, subunit ChlI; PFAM: magnesium chelatase ChlI subunit; ATPase associated with various cellular activities AAA_5.
 
   
 0.618
ADD69528.1
Regulatory protein RecX; Modulates RecA activity; Belongs to the RecX family.
  
  
 0.609
uvrA
Excinuclease ABC, A subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
   
 
 0.600
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 [...]
    
 0.595
uvrC
Excinuclease ABC, C subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
     
 0.589
Your Current Organism:
Denitrovibrio acetiphilus
NCBI taxonomy Id: 522772
Other names: D. acetiphilus DSM 12809, Denitrovibrio acetiphilus DSM 12809, Denitrovibrio acetiphilus N2460, Denitrovibrio acetiphilus str. DSM 12809, Denitrovibrio acetiphilus strain DSM 12809
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