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
hisShistidine--tRNA ligase; Identified by match to protein family HMM PF00587; match to protein family HMM PF03129; match to protein family HMM TIGR00442. (425 aa)    
Predicted Functional Partners:
aspS
aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
  
 0.921
EGJ26871.1
Putative cross-wall-targeting lipoprotein signal; Identified by match to protein family HMM PF00746; match to protein family HMM PF08363; match to protein family HMM TIGR01167; match to protein family HMM TIGR03726.
  
 
 0.728
glyQ
glycine--tRNA ligase, alpha subunit; Identified by match to protein family HMM PF02091; match to protein family HMM TIGR00388.
  
  
 0.726
thrS
threonine--tRNA ligase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr).
  
 
 0.691
serS
serine--tRNA ligase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec).
  
 
 0.671
alaS
alanine--tRNA ligase; 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.
  
 
 0.664
valS
valine--tRNA ligase; 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.
 
 
 0.660
lysS
lysine--tRNA ligase; Identified by match to protein family HMM PF00152; match to protein family HMM PF01336; match to protein family HMM TIGR00499; Belongs to the class-II aminoacyl-tRNA synthetase family.
   
 
 0.659
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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
 
 
 0.634
cysS
cysteine--tRNA ligase; Identified by match to protein family HMM PF01406; match to protein family HMM PF09190; match to protein family HMM PF09334; match to protein family HMM TIGR00435; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.617
Your Current Organism:
Streptococcus porcinus
NCBI taxonomy Id: 873448
Other names: S. porcinus str. Jelinkova 176, Streptococcus porcinus str. Jelinkova 176, Streptococcus porcinus strain Jelinkova 176
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.