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
pheTphenylalanyl-tRNA synthetase, beta subunit; Identified by match to protein family HMM PF01588; match to protein family HMM PF03147; match to protein family HMM PF03483; match to protein family HMM PF03484; match to protein family HMM TIGR00472; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (802 aa)    
Predicted Functional Partners:
pheS
phenylalanyl-tRNA synthetase, alpha subunit; Identified by match to protein family HMM PF01409; match to protein family HMM PF02912; match to protein family HMM TIGR00468; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
 
 0.999
ileS
isoleucine#tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
  
 
 0.972
rpsB
Ribosomal protein S2; Identified by match to protein family HMM PF00318; match to protein family HMM TIGR01011; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.970
ACN98172.1
leucyl-tRNA synthetase subunit beta (Leucine--tRNA ligasesubunit beta) (LeuRS); Identified by match to protein family HMM PF08264.
  
  
 0.966
leuS
leucyl-tRNA synthetase; Identified by match to protein family HMM PF00133; match to protein family HMM PF09334; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.966
rplO
Ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
  
 0.960
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
   
  
 0.956
rpoB
DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
  
 0.954
rpsC
Ribosomal protein S3; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation; Belongs to the universal ribosomal protein uS3 family.
  
 
 0.944
pyrD
Dihydroorotate dehydrogenase; Catalyzes the conversion of dihydroorotate to orotate.
  
  
 0.937
Your Current Organism:
Sulfurihydrogenibium azorense
NCBI taxonomy Id: 204536
Other names: Aquificaceae bacterium Az-Fu1, S. azorense Az-Fu1, Sulfurihydrogenibium azorense Az-Fu1, Sulfurihydrogenibium azorense str. Az-Fu1, Sulfurihydrogenibium azorense strain Az-Fu1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.