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
lueSPutative leucyl-tRNA synthetase; PMID: 1317842 best DB hits: BLAST: ddbj:BAB17162.1; (AP002868) putative leucyl-tRNA synthetase; E=0.0 embl:CAB77903.1; (AL161500) putative leucyl tRNA synthetase; E=0.0 gb:AAK04914.1; AE006315_3 (AE006315) leucyl-tRNA synthetase (EC; E=0.0 COG: TP0586; COG0495 Leucyl-tRNA synthetase; E=0.0 PFAM: PF00133; tRNA synthetases class I (I, L; E=1.4e-39; Belongs to the class-I aminoacyl-tRNA synthetase family. (950 aa)    
Predicted Functional Partners:
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.
  
 0.996
ileS
Probable 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 2 subfamily.
  
 0.971
valS
valyl-tRNA synthetase; 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.
   
 
0.920
pheT
phenylalanyl-tRNA synthetase beta chain; PMID: 2991205 best DB hits: BLAST: swissprot:P07395; SYFB_ECOLI PHENYLALANYL-TRNA SYNTHETASE BETA; E=3e-78 gb:AAG56700.1; AE005394_9 (AE005394) phenylalanine tRNA; E=6e-78 embl:CAA23565.1; (V00291) phenylalanyl-tRNA synthetase; E=3e-77 COG: pheT_2; COG0072 Phenylalanyl-tRNA synthetase beta subunit; E=3e-79 PFAM: PF01588; Putative tRNA binding domain; E=2.2e-05.
  
  
 0.908
thrS
threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
  
 
 0.843
argS
arginyl-tRNA synthetase; PMID: 2668891 best DB hits: BLAST: pir:G82121; arginyl-tRNA synthetase VC2074 [imported] - Vibrio; E=1e-69 swissprot:Q55486; SYR_SYNY3 ARGINYL-TRNA SYNTHETASE; E=5e-68 embl:CAC01600.1; (AJ269505) putative arginyl-tRNA synthetase; E=4e-66 COG: VC2074; COG0018 Arginyl-tRNA synthetase; E=1e-70 PFAM: PF00750; tRNA synthetases class I (R); E=5.7e-55.
  
 0.835
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.
  
 
 0.831
gltX
glutamyl-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.
  
 0.826
tyrS
tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.
  
 
 0.816
lysS
lysyl-tRNA synthetase; Best DB hits: BLAST: swissprot:Q53638; SYK_STAAU LYSYL-TRNA SYNTHETASE (LYSINE--TRNA; E=1e-116 swissprot:P37477; SYK_BACSU LYSYL-TRNA SYNTHETASE (LYSINE--TRNA; E=1e-114 swissprot:Q9KGG4; SYK_BACHD LYSYL-TRNA SYNTHETASE (LYSINE--TRNA; E=1e-111 COG: BS_lysS; COG1190 Lysyl-tRNA synthetase class II; E=1e-115 PFAM: PF01336; OB-fold nucleic acid binding dom; E=5.9e-12 PF01409; tRNA synthetases class II (F); E=0.46 PF00152; tRNA synthetases class II (D, K; E=7e-136; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.803
Your Current Organism:
Rhodopirellula baltica
NCBI taxonomy Id: 243090
Other names: Pirellula sp. 1, R. baltica SH 1, Rhodopirellula baltica SH 1, Rhodopirellula baltica str. SH 1, Rhodopirellula baltica strain SH 1
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