STRINGSTRING
alaS alaS pheT pheT leuS leuS valS valS metG metG thrS thrS ileS ileS aspS aspS glyQ glyQ glyS glyS secD secD
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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alaSalanyl-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. (874 aa)    
Predicted Functional Partners:
pheT
TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: pmy:Pmen_1981 phenylalanyl-tRNA synthetase subunit beta; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial.
 
 
 0.934
leuS
TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: pfl:PFL_5439 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.924
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.
 
  
 0.919
metG
Methionyl-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.
  
  
 0.907
thrS
threonyl-tRNA synthetase; 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).
  
 
 0.901
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.
 
 
 0.900
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.
 
  
 0.881
glyQ
PFAM: Glycyl-tRNA synthetase, class IIc, alpha subunit; TIGRFAM: Glycyl-tRNA synthetase, class IIc, alpha subunit; HAMAP: Glycyl-tRNA synthetase, class IIc, alpha subunit; KEGG: pap:PSPA7_0009 glycyl-tRNA synthetase subunit alpha.
  
  
 0.833
glyS
TIGRFAM: Glycyl-tRNA synthetase, class IIc, beta subunit; HAMAP: Glycyl-tRNA synthetase, class IIc, beta subunit; KEGG: pmy:Pmen_0013 glycyl-tRNA synthetase subunit beta.
  
  
 0.827
secD
Protein-export membrane protein SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
  
    0.821
Your Current Organism:
Pseudomonas fulva
NCBI taxonomy Id: 743720
Other names: P. fulva 12-X, Pseudomonas fulva 12-X, Pseudomonas fulva str. 12-X, Pseudomonas fulva strain 12-X
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