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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
rhlBRNA helicase; DEAD-box RNA helicase involved in RNA degradation. Has RNA- dependent ATPase activity and unwinds double-stranded RNA. Belongs to the DEAD box helicase family. RhlB subfamily. (429 aa)    
Predicted Functional Partners:
pnp
Polynucleotide phosphorylase/polyadenylase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
  
 
 0.790
gppA
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities.
  
    0.779
prfB
Peptide chain release factor 2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
  
 
 0.764
rplC
50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
   
 
 0.730
AMQ41029.1
Modulator protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.675
rplD
50S ribosomal protein L4; Forms part of the polypeptide exit tunnel.
   
 0.672
AMQ43619.1
GTPase; Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity; Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily.
  
 0.628
rplJ
50S ribosomal protein L10; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family.
   
 
 0.620
rplM
50S ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
   
 
 0.604
rplK
50S ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
   
 
 0.589
Your Current Organism:
Aeromonas veronii
NCBI taxonomy Id: 654
Other names: A. veronii, ATCC 35624, ATCC 49904 [[Aeromonas ichthiosmia]], Aeromonas culicicola, Aeromonas culicicola Pidiyar et al. 2002, Aeromonas hybridization group 10 (HG10), Aeromonas ichthiosmia, Aeromonas sp. G18, Aeromonas sp. R1, Aeromonas sp. R9, Aeromonas sp. TH074, Aeromonas sp. TH076, CCUG 27821, CECT 4257, CECT 4486 [[Aeromonas ichthiosmia]], CIP 103438, CIP 104613 [[Aeromonas ichthiosmia]], CIP 107763 [[Aeromonas culicicola]], DSM 6393 [[Aeromonas ichthiosmia]], DSM 7386, Enteric Group 77, JCM 7375, JCM 8354 [[Aeromonas ichthiosmia]], LMG 12645 [[Aeromonas ichthiosmia]], LMG:12645 [[Aeromonas ichthiosmia]], MTCC 3249 [[Aeromonas culicicola]], NCIMB 13205 [[Aeromonas ichthiosmia]], NICM 5147 [[Aeromonas culicicola]], strain 115/II [[Aeromonas ichthiosmia]]
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.