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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
aspSaspartate--tRNA ligase; 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. (604 aa)    
Predicted Functional Partners:
gatB
gatB: aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 
 
 0.986
alaS
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.
  
 0.916
gatC
gatC: aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
  
 
 0.881
hisS
hisS: histidine--tRNA ligase; TIGRFAM:TIGR00442:Histidine-tRNA ligase; COG:COG0124: Histidyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF13393:Histidyl-tRNA synthetase; Hamap:MF_00127:Histidine-tRNA ligase; PIRSF:PIRSF001549:Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit; ProSiteProfiles:PS50862:Aminoacyl-tRNA synthetase, class II; SUPERFAMILY:SSF55681:No Description;KEGG: 00970; Reactome: REACT_71.
 
  
 0.880
AHY46577.1
TIGR01033: DNA-binding regulatory protein, YebC/PmpR family; TIGRFAM:TIGR01033:Transcriptional regulator TACO1-like; COG:COG0217: Uncharacterized conserved protein [Function unknown]; Pfam:PF01709:Transcriptional regulator TACO1-like; Hamap:MF_00693:Transcriptional regulator TACO1-like; SUPERFAMILY:SSF75625:No Description.
  
 0.828
pheT
TIGRFAM:TIGR00472:Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial; COG:COG0072: Phenylalanyl-tRNA synthetase beta subunit [Translation ribosomal structure and biogenesis]; Pfam:PF03483:B3/B4 tRNA-binding domain; Hamap:MF_00283:Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial; ProSiteProfiles:PS51483:tRNA synthetase, B5-domain; SMART:SM00873:B3/B4 tRNA-binding domain; SUPERFAMILY:SSF56037:Phenylalanyl-tRNA synthetase, B3/B4;KEGG: 00970; pheT_bact.
 
  
 0.819
guaA
GMP synthase (glutamine-hydrolyzing), C-terminal domain; Catalyzes the synthesis of GMP from XMP.
  
  
 0.808
valS
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.
 
  
 0.788
metG
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.
 
 
 0.772
leuS
TIGRFAM:TIGR00396:Leucine-tRNA ligase, bacterial/mitochondrial; COG:COG0495: Leucyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF13603:Leucyl-tRNA synthetase, editing domain; Hamap:MF_00049_B:Leucine-tRNA ligase, bacterial/mitochondrial; PRINTS:PR00985:Leucine-tRNA ligase, bacterial/mitochondrial; SUPERFAMILY:SSF52374:No Description;KEGG: 00290; KEGG: 00970; leuS_bact; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.760
Your Current Organism:
Rubrobacter radiotolerans
NCBI taxonomy Id: 42256
Other names: ATCC 51242, Arthrobacter radiotolerans, CIP 106991, DSM 46359, DSM 5868, IAM 12072, IFO 14777, JCM 2153, NBRC 14777, R. radiotolerans, strain P-1
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