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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colored nodes:
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ACE03864.1PFAM: peptidase S24 and S26 domain protein; KEGG: plt:Plut_1201 SOS-response transcriptional repressors (RecA-mediated autopeptidase)-like. (150 aa)    
Predicted Functional Partners:
ACE03865.1
DNA-directed DNA polymerase; PFAM: UMUC domain protein DNA-repair protein; KEGG: pvi:Cvib_0129 DNA-directed DNA polymerase.
 
 0.993
recA
recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
  
 0.970
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.
  
 
 0.772
ACE02991.1
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 [...]
  
 
 0.720
ACE04644.1
PFAM: Exonuclease RNase T and DNA polymerase III; SMART: Exonuclease; KEGG: plt:Plut_0528 exonuclease.
  
 
 0.719
ACE05060.1
KEGG: ppd:Ppro_2346 DNA-directed DNA polymerase; PFAM: Exonuclease RNase T and DNA polymerase III; SMART: Exonuclease.
  
 
 0.719
ACE03745.1
PFAM: UvrD/REP helicase; KEGG: pvi:Cvib_0501 ATP-dependent DNA helicase PcrA.
     
 0.715
ACE04344.1
PFAM: NERD domain protein; KEGG: aoe:Clos_2030 NERD domain protein.
     
 0.715
ACE04483.1
PFAM: UvrD/REP helicase; KEGG: ppg:PputGB1_3118 UvrD/REP helicase; Belongs to the helicase family. UvrD subfamily.
     
 0.713
ACE04484.1
KEGG: ppg:PputGB1_3117 hypothetical protein.
     
 0.713
Your Current Organism:
Chlorobium phaeobacteroides BS1
NCBI taxonomy Id: 331678
Other names: C. phaeobacteroides BS1, Chlorobium phaeobacteroides MN1, Chlorobium phaeobacteroides str. BS1, Chlorobium phaeobacteroides strain BS1
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