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pheS protein (Staphylococcus carnosus) - STRING interaction network
"pheS" - Phenylalanine--tRNA ligase alpha subunit in Staphylococcus carnosus
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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pheSPhenylalanine--tRNA ligase alpha subunit; (Q99QR1) Phenylalanyl-tRNA synthetase alpha chain (EC 6.1.1.20) (Phenylalanine--tRNA ligase alpha chain) (PheRS),InterPro- Phenylalanyl-tRNA synthetase alpha subunit; Hypothetical protein; Sca_0756; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily (352 aa)    
Predicted Functional Partners:
pheT
Phenylalanine--tRNA ligase beta subunit; (Q8CSY8) Phenylalanyl-tRNA synthetase beta chain (EC 6.1.1.20) (Phenylalanine--tRNA ligase beta chain) (PheRS),InterPro- Bacterial phenylalanyl-tRNA synthetase beta subunit; Hypothetical protein; Sca_0757 (801 aa)
  0.999
metS
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 (667 aa)
 
 
  0.967
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 (876 aa)
 
   
  0.859
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (513 aa)
 
   
  0.859
hisS
Histidine--tRNA ligase; Similar to histidyl-tRNA synthetase hisS (EC 6.1.1.21),,Bacillus subtilis, 424AA, Expect = 1e-141,Identities = 244/412 (59%), Positives = 319/412 (77%),Gaps = 1/412 (0%),(P60909) Histidyl-tRNA synthetase (EC 6.1.1.21) (Histidine--tRNA ligase) (HisRS),InterPro- Histidyl-tRNA synthetase class IIa; Hypothetical protein; Sca_1242 (428 aa)
 
 
  0.843
lysS
Lysine--tRNA ligase; (Q8CQV5) Lysyl-tRNA synthetase (EC 6.1.1.6) (Lysine--tRNA ligase) (LysRS),InterPro- Lysyl-tRNA synthetase class-2; Hypothetical protein; Sca_0169; Belongs to the class-II aminoacyl-tRNA synthetase family (497 aa)
 
   
  0.826
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 (588 aa)
     
   
  0.814
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 (876 aa)
 
   
  0.791
fusA
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (693 aa)
 
 
  0.784
lepA
Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner (607 aa)
 
   
  0.777
Your Current Organism:
Staphylococcus carnosus
NCBI taxonomy Id: 396513
Other names: S. carnosus subsp. carnosus TM300, Staphylococcus carnosus, Staphylococcus carnosus subsp. carnosus TM300, Staphylococcus carnosus subsp. carnosus str. TM300, Staphylococcus carnosus subsp. carnosusstrain TM300
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