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
glyQGlycine--tRNA ligase; PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: son:SO0015 glycyl-tRNA synthetase alpha chain. (301 aa)    
Predicted Functional Partners:
glyS
Glycine--tRNA ligase; KEGG: son:SO0014 glycyl-tRNA synthetase beta chain.
 0.999
hisS
KEGG: son:SO3311 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein.
  
  
 0.789
Sfri_0548
Carbamoyl-phosphate synthase L chain, ATP-binding; PFAM: biotin/lipoyl attachment domain-containing protein; ATP-dependent carboxylate-amine ligase domain protein, ATP-grasp; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: son:SO0840 acetyl-CoA carboxylase multifunctional enzyme accADC, carboxyl transferase subunit alpha/carboxyl transferase subunit beta/biotin carboxylase.
   
  
 0.702
alaS
alanyl-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.
   
  
 0.700
pheS
KEGG: son:SO2085 phenylalanyl-tRNA synthetase alpha chain; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase, class IIc; aminoacyl tRNA synthetase, class II domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
   
  
 0.686
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
    0.656
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.
 
  
 0.653
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.
  
  
 0.629
atpH
ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
   
    0.611
aspS
aspartyl-tRNA synthetase; 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.
  
  
 0.608
Your Current Organism:
Shewanella frigidimarina
NCBI taxonomy Id: 318167
Other names: S. frigidimarina NCIMB 400, Shewanella frigidimarina NCIMB 400, Shewanella frigidimarina str. NCIMB 400, Shewanella frigidimarina strain NCIMB 400
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.