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
metGmethionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (702 aa)    
Predicted Functional Partners:
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: plt:Plut_1636 leucyl-tRNA synthetase, class Ia; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
0.991
pheS
KEGG: plt:Plut_0119 phenylalanyl-tRNA synthetase, alpha subunit; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase, class IIc; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
  
 
 0.967
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 2 subfamily.
 
 0.943
gltX
glutamyl-tRNA synthetase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
 
 0.943
Cvib_0382
Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
  
 
 0.932
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
  
 
 0.932
proS
prolyl-tRNA synthetase; 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).
 
 0.901
argS
KEGG: plt:Plut_2092 arginyl-tRNA synthetase, class Ic; TIGRFAM: arginyl-tRNA synthetase.
  
 0.887
pheT
TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: plt:Plut_0711 phenylalanyl-tRNA synthetase, beta subunit.
  
  
 0.871
lysS
TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type; KEGG: plt:Plut_1357 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.836
Your Current Organism:
Chlorobium phaeovibrioides
NCBI taxonomy Id: 290318
Other names: C. phaeovibrioides DSM 265, Chlorobium phaeovibrioides DSM 265, Chlorobium vibrioforme f. thiosulfatophilum DSM 265, Prosthecochloris vibrioformis DSM 265
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