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
rnhBRibonuclease HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (201 aa)    
Predicted Functional Partners:
AFD05518.1
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 [...]
  
 
 0.926
rnhA
Ribonuclease HI; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids; Belongs to the RNase H family.
   
 
 0.870
AFD07892.1
lipid-A-disaccharide synthase; Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
  
  
 0.863
AFD06342.1
Topoisomerase IB; PFAM: Eukaryotic DNA topoisomerase I, catalytic core.
    
 
 0.858
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
  
 
 0.857
AFD06723.1
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: AMP-binding enzyme.
  
   0.828
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]
    
 
 0.814
AFD07466.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain.
    
 
 0.814
AFD08233.1
Hypothetical protein.
       0.773
AFD06309.1
DNA polymerase elongation subunit (family B); PFAM: Predicted 3'-5' exonuclease related to the exonuclease domain of PolB.
   
 
 0.759
Your Current Organism:
Solitalea canadensis
NCBI taxonomy Id: 929556
Other names: S. canadensis DSM 3403, Solitalea canadensis DSM 3403, Solitalea canadensis IFO 15130, Solitalea canadensis NBRC 15130, Solitalea canadensis str. DSM 3403, Solitalea canadensis strain DSM 3403
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.