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
glyQglycyl-tRNA synthetase, alpha subunit; Identified by similarity to SP:P00960; match to protein family HMM PF02091; match to protein family HMM TIGR00388. (311 aa)    
Predicted Functional Partners:
glyS
glycyl-tRNA synthetase, beta subunit; Identified by similarity to SP:P00961; match to protein family HMM PF02092; match to protein family HMM PF05746; match to protein family HMM TIGR00211.
 0.999
SPO1356a
Signal transduction; 'Novel gene detected by proteogenomics, SPO_PG019; identified in over 20 other Roseobacter strains'.
 
 
 0.994
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
  
  
 0.811
hisS
histidyl-tRNA synthetase.
  
  
 0.782
ileS
isoleucyl-tRNA synthetase; 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.
 
  
 0.729
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.
   
  
 0.706
SPO1354
Peptidoglycan binding domain protein; Identified by match to protein family HMM PF01471.
       0.697
SPO1356
Methyltransferase, FkbM family; Identified by match to protein family HMM TIGR01444.
       0.689
valS
valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
   
  
 0.647
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.645
Your Current Organism:
Ruegeria pomeroyi
NCBI taxonomy Id: 246200
Other names: R. pomeroyi DSS-3, Ruegeria pomeroyi DSS-3, Ruegeria pomeroyi str. DSS-3, Ruegeria pomeroyi strain DSS-3, Silicibacter pomeroyi DSS-3
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.