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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
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[Homology]
Score
alaSalanyl-tRNA synthetase (alaS); 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. (882 aa)    
Predicted Functional Partners:
pheT
phenylalanyl-tRNA synthetase beta chain (pheT); Psort: bacterial inner membrane --- Certainty= 0.193(Affirmative); COG0072 PheT phenylalanyl-tRNA synthetase beta subunit.
  
 
 0.907
ileS
isoleucine-tRNA ligase (ileS); 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.
  
 
 0.866
leuS
leucyl-tRNA synthetase (leuS); Psort: bacterial cytoplasm --- Certainty= 0.485(Affirmative); COG0495 leuS leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.861
valS
valyl-tRNA synthetase (valS); 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.
  
  
 0.859
thrS
Threonyl-tRNA synthetase (thrS); 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).
  
 
 0.820
metS
methionyl-tRNA synthetase (metS); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
 
  
 0.778
glyQ
glycyl-tRNA synthetase alpha subunit (glyQ); Psort: bacterial cytoplasm --- Certainty= 0.269(Affirmative); COG0752 GlyQ glycyl-tRNA synthetase, alpha subunit.
   
  
 0.742
glyS
glycyl-tRNA synthetase beta chain (glyS); Psort: bacterial inner membrane --- Certainty= 0.179(Affirmative); COG0751 GlyS glycyl-tRNA synthetase, beta subunit.
   
  
 0.728
thiF
Thiamine biosynthesis protein (thiF); Psort: bacterial outside --- Certainty= 0.300(Affirmative); COG0476 ThiF dinucleotide-utilizing enzymes involved in molybdopterin and thiamine biosynthesis family 2.
   
  0.723
aspS
aspartyl-tRNA synthetase (aspS); 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.
  
  
 0.705
Your Current Organism:
Anaplasma marginale
NCBI taxonomy Id: 320483
Other names: A. marginale str. Florida, Anaplasma marginale str. Florida, Anaplasma marginale strain Florida
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