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
leuSTIGRFAM: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. (815 aa)    
Predicted Functional Partners:
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.
  
 0.996
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.
  
  
 0.993
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
   
 
 0.992
ileS
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 2 subfamily.
 
0.934
argS
argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71.
  
 0.877
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.
  
 
0.852
gltX
Glutamyl- and glutaminyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 0.840
gltX-2
glutamate--tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 0.840
proS
proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
  
 0.809
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.
 
 
 0.806
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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