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R2601_04773 protein (Pelagibaca bermudensis) - STRING interaction network
"R2601_04773" - Ribonuclease BN in Pelagibaca bermudensis
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
R2601_04773Ribonuclease BN (313 aa)    
Predicted Functional Partners:
R2601_00255
FAD linked oxidase (946 aa)
 
 
      0.587
rph
tRNA nucleotidyltransferase ; Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates (237 aa)
       
  0.577
rnd
Ribonuclease D ; Exonuclease involved in the 3’ processing of various precursor tRNAs. Initiates hydrolysis at the 3’-terminus of an RNA molecule and releases 5’-mononucleotides (385 aa)
         
    0.576
rne
Ribonuclease E ; Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs (985 aa)
       
    0.575
R2601_09320
Ribonuclease, Rne/Rng family protein (283 aa)
       
    0.575
R2601_04763
Glucose dehydrogenase (741 aa)
         
  0.502
R2601_04768
Uncharacterized protein (103 aa)
              0.502
R2601_19337
Uncharacterized protein (274 aa)
 
          0.499
dtd
D-aminoacyl-tRNA deacylase ; D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo (146 aa)
   
        0.468
map
Peptidase M ; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (282 aa)
         
  0.463
Your Current Organism:
Pelagibaca bermudensis
NCBI taxonomy Id: 314265
Other names: P. bermudensis HTCC2601, Pelagibaca, Pelagibaca Cho and Giovannoni 2006, Pelagibaca bermudensis, Pelagibaca bermudensis Cho and Giovannoni 2006, Pelagibaca bermudensis HTCC2601, Pelagibaca bermudensis str. HTCC2601, Pelagibaca bermudensis strain HTCC2601, Roseovarius sp. HTCC2601
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