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
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[Homology]
Score
ywqLPutative deoxyribonuclease 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. (238 aa)    
Predicted Functional Partners:
ywqI
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
  
 0.972
rttO
Putative ribonuclease antitoxin; Probable antitoxin component of a type II toxin-antitoxin (TA) system. Probably neutralizes the ability to inhibit growth of cognate toxin YwqJ. Probably does not have antitoxin activity on other toxins with the LXG toxin domain (By similarity).
 
  
 0.965
rttN
Putative ribonuclease toxin; Probable toxic component of a type II toxin-antitoxin (TA) system. The C-terminus may have RNase activity and probably inhibits growth. Its toxic effects are probably neutralized by its cognate antitoxin YwqK, but not by antitoxins specific to other toxins with the LXG domain (By similarity).
  
  
 0.960
ywqH
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 15101989.
  
  
 0.899
nfo
Type IV apurinic/apyrimidinic endonuclease; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
      
 0.790
yxiC
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
   
  
 0.783
mutM
formamidopyrimidine-DNA glycosidase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidi [...]
    
 
 0.778
yxxE
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
   
  
 0.767
ung
uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine; Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family.
      
 0.758
alkA
DNA-3-methyladenine glycosylase; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine and 7- methylguanine from the damaged DNA polymer formed by alkylation lesions.
      
 0.707
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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