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
OGV35373.1poly(A) polymerase; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. (372 aa)    
Predicted Functional Partners:
OGV35374.1
2-amino-4-hydroxy-6- hydroxymethyldihydropteridine diphosphokinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
    0.981
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
    
 0.874
cca
2',3'-cyclic phosphodiesterase; 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. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
 
  
 
0.702
A3E88_03565
Hypothetical protein; Metagenomic; derived from metagenome: subsurface metagenome.
   
 0.699
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.
   
 
  0.665
OGV30938.1
biotin--[acetyl-CoA-carboxylase] ligase; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
  
 0.654
birA
biotin--[acetyl-CoA-carboxylase] ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
  
  
 0.654
rnr
Ribonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
  
 0.608
metG
methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
 
 
 0.566
glmM
Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the phosphohexose mutase family.
      0.523
Your Current Organism:
Legionellales bacterium RIFCSPHIGHO212FULL3511
NCBI taxonomy Id: 1798567
Other names: L. bacterium RIFCSPHIGHO2_12_FULL_35_11, Legionellales bacterium RIFCSPHIGHO2_12_FULL_35_11
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.