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.
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[Homology]
Score
KOH22297.1DNA helicase IV; Derived by automated computational analysis using gene prediction method: Protein Homology. (689 aa)    
Predicted Functional Partners:
xni
Protein Xni; Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment.
 
 
 
 0.816
recA
Catalyzes 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; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.785
dnaN
DNA polymerase III subunit beta; 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 [...]
  
 
 0.733
uvrC
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; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.708
recQ
ATP-dependent DNA helicase RecQ; Functions in blocking illegitimate recombination, enhancing topoisomerase activity, initiating SOS signaling and clearing blocked replication forks; component of the RecF recombinational pathway; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.696
KOH18386.1
ATP-dependent DNA helicase RecQ; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.696
ligA
NAD-dependent DNA ligase LigA; This protein catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction; essential for DNA replication and repair of damaged DNA; similar to ligase LigB; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.674
aroE
Shikimate dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
  
  
 0.668
KOH17348.1
3-hydroxyisobutyrate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.663
serB
Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
      
 0.661
Your Current Organism:
Vibrio parahaemolyticus
NCBI taxonomy Id: 670
Other names: ATCC 17802, Beneckea parahaemolytica, CAIM 320, CCUG 14474, CCUG 15657, CCUG 4224, CIP 75.2, DSM 10027, IFO 12711, LMG 2850, LMG:2850, NBRC 12711, NCCB 77010, NCCB 77018, NCTC 10903, NRRL B-4167, Oceanomonas parahaemolytica, Pasteurella parahaemolytica, V. parahaemolyticus
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