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
leuSHypothetical protein; Similarity to COG0495 Leucyl-tRNA synthetase(Evalue: 0); Belongs to the class-I aminoacyl-tRNA synthetase family. (827 aa)    
Predicted Functional Partners:
metG
Hypothetical protein; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
 
0.997
pheT
Hypothetical protein; Similarity to COG0072 Phenylalanyl-tRNA synthetase beta subunit(Evalue: 1E-135).
  
  
 0.994
gltX
Hypothetical protein; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
 
 0.967
argS
Hypothetical protein; Similarity to COG0018 Arginyl-tRNA synthetase(Evalue: 1E-158).
  
 0.941
ileS
Hypothetical protein; 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.
 
0.930
proS
Hypothetical protein; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...]
 
 0.922
glnS
Hypothetical protein; Similarity to COG0008 Glutamyl- and glutaminyl-tRNA synthetases(Evalue: 0).
  
 0.918
asnS
Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162).
 
 0.916
valS
Hypothetical protein; 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.
  
 
0.913
thrS
Hypothetical protein; 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).
 
 
 0.905
Your Current Organism:
Desulfitobacterium hafniense
NCBI taxonomy Id: 138119
Other names: D. hafniense Y51, Desulfitobacterium hafniense Y51, Desulfitobacterium hafniense str. Y51, Desulfitobacterium hafniense strain Y51, Desulfitobacterium sp. Y51
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