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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
KLV27954.1methionyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. (546 aa)    
Predicted Functional Partners:
leuS
leucyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.871
pheT
phenylalanyl-tRNA synthase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.834
KLV18550.1
isoleucyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.819
KLV18553.1
aspartyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.798
asnC
asparagine--tRNA ligase; Catalyzes a two-step reaction, first charging an asparagine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.764
KLV28518.1
arginine--tRNA ligase; Catalyzes a two-step reaction, first charging an arginine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class-I aminoacyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.762
glnS
glutamate--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.751
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).
  
 0.751
proS
prolyl-tRNA synthetase; 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]
  
 0.710
proS-2
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).
  
 0.710
Your Current Organism:
Bacillus circulans
NCBI taxonomy Id: 1397
Other names: ATCC 24, ATCC 4513, ATCC 9140, B. circulans, BCRC 10605, Bacillus sp. 3399BRRJ, Bacillus sp. NCIM 2107, Bacillus sp. NCIM 5045, Bacillus sp. NCIM 5046, CCM 2048, CCRC 10605, CCRC:10605, CCUG 7416, CIP 52.75, DSM 11, IAM 12462, IFO 13626, JCM 2504, LMG 13261, LMG 6926, LMG:13261, LMG:6926, NBRC 13626, NCCB 75011, NCIB 9374, NCIMB 9374, NCTC 2610, NRRL B-378, NRRL B-380
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