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
ungUracil-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. (220 aa)    
Predicted Functional Partners:
xthA
Similar to Q83EM1 Exodeoxyribonuclease III from Coxiella burnetii (259 aa). FASTA: opt: 991 Z-score: 1173.5 E(): 1.6e-57 Smith-Waterman score: 991; 54.789 identity in 261 aa overlap.
   
 0.862
FTT_1579c
Similar to O25314 Type III restriction enzyme R protein from Helicobacter pylori (1001 aa). FASTA: opt: 1491 Z-score: 1485.7 E(): 6.6e-75 Smith-Waterman score: 2480; 42.828 identity in 990 aa overlap ORF ftt1579c.
  
    0.785
nth
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate.
  
 
 0.709
dnaN
DNA polymerase III, beta chain; 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 r [...]
   
 
 0.577
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
  
  
 0.571
dut
dUTP pyrophosphatase (Deoxyuridine 5'-triphosphate nucleotidohydrolase); This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family.
  
 
 0.489
FTT_1580c
Identical to AAP83333 Hypothetical protein from Francisella tularensis ssp. tularensis strain SchuS4 (FSC237) (176 aa). ORF ftt1580c.
       0.428
tadA
Zinc-binding domain protein; Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2); Belongs to the cytidine and deoxycytidylate deaminase family.
  
 
 0.408
recA
Recombinase A 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.
   
 
 0.407
Your Current Organism:
Francisella tularensis SCHUS4
NCBI taxonomy Id: 177416
Other names: F. tularensis subsp. tularensis SCHU S4, Francisella tularensis Biovar A str. SCHU S4, Francisella tularensis Biovar A str. Schu 4, Francisella tularensis subsp. tularensis SCHU S4, Francisella tularensis subsp. tularensis Schu 4, Francisella tularensis subsp. tularensis str. SCHU S4, Francisella tularensis subsp. tularensis strain SCHU S4
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