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
valSvaline--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. (874 aa)    
Predicted Functional Partners:
leuS
leucine--tRNA ligase; KEGG: gka:GK2842 1.9e-288 leuS; leucyl-tRNA synthetase K01869; COG: COG0495 Leucyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.98; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
0.909
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). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
 
0.891
pheT
KEGG: gka:GK2706 2.3e-157 phenylalanyl-tRNA synthetase beta subunit K01890; COG: COG0073 EMAP domain; Psort location: Cytoplasmic, score:9.98.
  
  
 0.855
ppiB
Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
  
 
 0.826
guaA
GMP synthase (glutamine-hydrolyzing) domain protein; Catalyzes the synthesis of GMP from XMP.
  
  
 0.818
guaA-2
GMP synthase (glutamine-hydrolyzing) domain protein; KEGG: bth:BT2419 8.9e-179 putative GMP synthase [glutamine-hydrolyzing] K01951; COG: COG0518 GMP synthase - Glutamine amidotransferase domain; Psort location: Cytoplasmic, score:8.87.
  
  
 0.818
hisS
histidine--tRNA ligase; KEGG: btl:BALH_3985 1.9e-112 hisS; histidine--tRNA ligase K01891; COG: COG0124 Histidyl-tRNA synthetase; Psort location: Cytoplasmic, score:10.00.
 
 
 0.798
EDP10718.1
Acetyltransferase, GNAT family; KEGG: btk:BT9727_2749 1.8e-15 ribosomal-protein-alanine acetyltransferase K00676; COG: COG1670 Acetyltransferases, including N-acetylases of ribosomal proteins; Psort location: Cytoplasmic, score:8.87.
  
    0.786
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.
 
  
 0.770
metG
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.
  
 
0.765
Your Current Organism:
Absiella dolichum
NCBI taxonomy Id: 428127
Other names: A. dolichum DSM 3991, Absiella dolichum ATCC 29143, Absiella dolichum DSM 3991, Eubacterium dolichum ATCC 29143, Eubacterium dolichum DSM 3991, Eubacterium dolichum strain DSM 3991
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