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
proSproline--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). (479 aa)    
Predicted Functional Partners:
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.
   
 0.987
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.
  
 0.950
argS
arginine--tRNA ligase; KEGG: bld:BLi03971 2.1e-170 argS; arginyl-tRNA synthetase; RBL01630 K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score: 9.98.
  
 0.943
gltX
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).
  
 0.927
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.
  
 0.927
asnS
asparagine--tRNA ligase; KEGG: ctc:CTC00143 9.4e-152 asparaginyl-tRNA synthetase K01893; COG: COG0017 Aspartyl/asparaginyl-tRNA synthetases; Psort location: Cytoplasmic, score: 10.00.
  
 
 0.911
leuS
leucine--tRNA ligase; KEGG: gka:GK2842 0. 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.
  
 0.888
lysS
lysine--tRNA ligase; KEGG: gka:GK0074 3.2e-167 lysyl-tRNA synthetase (lysine--tRNA ligase) K04567; COG: COG1190 Lysyl-tRNA synthetase (class II); Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.867
EDS73814.1
TIM-barrel protein, nifR3 family; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family.
  
 
 0.795
pheT
KEGG: gka:GK2706 2.5e-151 phenylalanyl-tRNA synthetase beta subunit K01890; COG: COG0073 EMAP domain; Psort location: Cytoplasmic, score: 9.98.
  
 
 0.753
Your Current Organism:
Clostridium spiroforme
NCBI taxonomy Id: 428126
Other names: Clostridium spiroforme ATCC 29900, [. spiroforme DSM 1552, [Clostridium] spiroforme DSM 1552
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.