STRINGSTRING
leuS protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"leuS" - Leucine--tRNA ligase in Desulfovibrio vulgaris Hildenborough
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
leuSLeucine--tRNA ligase; Identified by similarity to SP-P07813; match to protein family HMM PF00133; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family (829 aa)    
Predicted Functional Partners:
trmE
tRNA modification GTPase MnmE; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- like GTPase superfamily. TrmE GTPase family (457 aa)
   
  0.963
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) (938 aa)
 
 
0.955
argS
Arginine--tRNA ligase; Identified by similarity to SP-P35868; match to protein family HMM PF00750; match to protein family HMM PF03485; match to protein family HMM PF05746; match to protein family HMM TIGR00456 (551 aa)
     
 
  0.953
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). Also edits incorrectly charged L-seryl-tRNA(Thr) (644 aa)
 
 
  0.940
asnS
Asparagine--tRNA ligase; Identified by similarity to SP-P17242; match to protein family HMM PF00152; match to protein family HMM PF01336; match to protein family HMM TIGR00457 (461 aa)
   
 
  0.934
cysS
Cysteine--tRNA ligase; Identified by similarity to SP-Q06752; match to protein family HMM PF01406; match to protein family HMM TIGR00435; Belongs to the class-I aminoacyl-tRNA synthetase family (485 aa)
 
 
  0.922
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 (879 aa)
 
 
  0.918
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) (424 aa)
 
   
  0.916
trpS
Tryptophanyl-tRNA synthetase; Identified by match to protein family HMM PF00579; match to protein family HMM TIGR00233; Belongs to the class-I aminoacyl-tRNA synthetase family (329 aa)
 
   
  0.914
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 (884 aa)
     
 
0.904
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
Server load: low (21%) [HD]