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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
rimASimilar to Escherichia coli 50S ribosomal protein L34 RpmH SW:RL34_ECOLI (P02437) (46 aa) fasta scores: E(): 4.8e-19, 95.7% id in 46 aa, and to Proteus mirabilis 50S ribosomal protein L34 RpmH SW:RL34_PROMI (P22836) (47 aa) fasta scores: E(): 3.8e-18, 93.3% id in 45 aa; Belongs to the bacterial ribosomal protein bL34 family. (46 aa)    
Predicted Functional Partners:
rnpA
Ribonuclease P protein; 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.
  
  
 0.995
rpmB
Similar to Escherichia coli 50S ribosomal protein L28 RpmB SW:RL28_ECOLI (P02428) (77 aa) fasta scores: E(): 1.1e-32, 92.2% id in 77 aa; Belongs to the bacterial ribosomal protein bL28 family.
   
 
 0.994
b0023
30S ribosomal protein S20; Binds directly to 16S ribosomal RNA.
  
 
 0.994
rplU
50S ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
  
 
 0.994
rpsU
30S ribosomal protein S21; Identical to Escherichia coli and Salmonella typhimurium 30S ribosomal protein S21 RpsU SW:RS21_ECOLI (P02379) (70 aa) fasta scores: E(): 2.3e-27, 100.0% id in 70 aa, and to Buchnera aphidicola (subsp Acyrthosiphon pisum) 30S ribosomal protein S21 RpsU TR:BAB12780 (EMBL:AP001118) (71 aa) fasta scores: E(): 1e-25, 90.1% id in 71 aa; Belongs to the bacterial ribosomal protein bS21 family.
   
 
 0.993
rpsN
30S ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
  
 
 0.992
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.
  
 
 0.992
rpsl
30S ribosomal protein S12; With S4 and S5 plays an important role in translational accuracy.
   
 
 0.991
rpmI
Similar to Escherichia coli 50S ribosomal protein L35 RpmI SW:RL35_ECOLI (P07085) (64 aa) fasta scores: E(): 1.8e-25, 89.1% id in 64 aa, and to Haemophilus influenzae 50S ribosomal protein L35 RpmI SW:RL35_HAEIN (P45519) (64 aa) fasta scores: E(): 1.2e-21, 81.3% id in 64 aa; Belongs to the bacterial ribosomal protein bL35 family.
  
 
 0.991
rpmG
50S ribosomal protein L33; Similar to Escherichia coli and Salmonella typhimurium 50S ribosomal protein L33 SW:RL33_ECOLI (P02436) (54 aa) fasta scores: E(): 1.7e-21, 96.3% id in 54 aa; Belongs to the bacterial ribosomal protein bL33 family.
   
 
 0.990
Your Current Organism:
Yersinia pestis
NCBI taxonomy Id: 214092
Other names: Y. pestis CO92, Yersinia pestis CO92, Yersinia pestis str. CO92, Yersinia pestis strain CO92
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.