STRINGSTRING
STRING protein interaction network
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
nucSHypothetical protein, conserved, DUF91 family; Cleaves both 3' and 5' ssDNA extremities of branched DNA structures; Belongs to the NucS endonuclease family. (252 aa)    
Predicted Functional Partners:
radA
RadA/Rad51 recombinase; Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity).
   
 
 0.940
nfi
Endonuclease V; DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
      
 0.817
TK1250
intein/rRNA intron-related DNA endonuclease.
      
 0.792
hjc
Archaeal type Holliday junction resolvase; A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.
  
   
 0.773
TK1819
Capsular polysaccharide biosynthesis protein.
      
 0.769
fen
Flap structure-specific endonuclease; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair [...]
      
 0.747
TK1900
Calcium-gated potassium channel protein.
 
     0.589
rfcS
Replication factor C, small subunit; Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA; Belongs to the activator 1 small subunits family. RfcS subfamily.
    
 
 0.580
pcn1
DNA polymerase sliding clamp; Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication. Belongs to the PCNA family.
  
 
 
 0.547
TK0808
Hypothetical protein, conserved; Binds to the DNA polymerase sliding clamp (PCNA) and dissociates the PCNA trimeric ring, leading to the inhibition of PCNA- dependent activities. In vitro, inhibits the PCNA-dependent activities of DNA polymerase PolB and of flap endonuclease 1 (FEN-1).
      
 0.481
Your Current Organism:
Thermococcus kodakarensis
NCBI taxonomy Id: 69014
Other names: Pyrococcus sp. (strain KOD1), Pyrococcus sp. KOD1, T. kodakarensis KOD1, Thermococcus kodakaraensis KOD1, Thermococcus kodakarensis KOD1, Thermococcus kodakarensis str. KOD1, Thermococcus kodakarensis strain KOD1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.