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
rnrRibonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. (790 aa)    
Predicted Functional Partners:
smpB
SsrA-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to [...]
    
 0.948
OFI49477.1
ADP-ribose pyrophosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.939
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
   
 
 0.814
OFI49739.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.802
rnpA
Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
     
 0.759
OFI48705.1
30S ribosomal protein S1; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.735
cca
CCA tRNA nucleotidyltransferase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.
  
 0.730
OFI48234.1
ABC transporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.725
rnj
RNase J family beta-CASP ribonuclease; An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
  
 
 0.687
OFI49447.1
Preprotein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
  
  
 0.671
Your Current Organism:
Floricoccus tropicus
NCBI taxonomy Id: 1859473
Other names: Anthococcus sp. DF1, F. tropicus, Floricoccus tropicus Chuah et al. 2017, JCM 31733, LMG 29833, LMG:29833, Lactobacillales bacterium DF1, Lactobacillales bacterium HibF2, Lactobacillales bacterium HibF5, Streptococcus sp. DF1, Streptococcus sp. HibF2, Streptococcus sp. HibF5, strain DF1
Server load: low (8%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.