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.
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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
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[Homology]
Score
alaSalanyl-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. (874 aa)    
Predicted Functional Partners:
valS
valyl-tRNA synthase; 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.
 
  
 0.936
pheT
phenylalanine--tRNA ligase; Catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a tetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 2 subfamily; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
 
 0.925
AMQ44484.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.914
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.
  
  
 0.905
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.
 
 
 0.890
thrS
threonine--tRNA ligase; 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).
  
 
 0.884
AMQ41921.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.882
leuS
leucine--tRNA ligase; LeuRS; class-I aminoacyl-tRNA synthetase; charges leucine by linking carboxyl group to alpha-phosphate of ATP and then transfers aminoacyl-adenylate to its tRNA; due to the large number of codons that tRNA(Leu) recognizes, the leucyl-tRNA synthetase does not recognize the anticodon loop of the tRNA, but instead recognition is dependent on a conserved discriminator base A37 and a long arm; an editing domain hydrolyzes misformed products; in Methanothermobacter thermautotrophicus this enzyme associates with prolyl-tRNA synthetase; Derived by automated computational [...]
 
 
 0.877
aspS
aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
  
 0.851
glyQ
glycyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.842
Your Current Organism:
Aeromonas veronii
NCBI taxonomy Id: 654
Other names: A. veronii, ATCC 35624, ATCC 49904 [[Aeromonas ichthiosmia]], Aeromonas culicicola, Aeromonas culicicola Pidiyar et al. 2002, Aeromonas hybridization group 10 (HG10), Aeromonas ichthiosmia, Aeromonas sp. G18, Aeromonas sp. R1, Aeromonas sp. R9, Aeromonas sp. TH074, Aeromonas sp. TH076, CCUG 27821, CECT 4257, CECT 4486 [[Aeromonas ichthiosmia]], CIP 103438, CIP 104613 [[Aeromonas ichthiosmia]], CIP 107763 [[Aeromonas culicicola]], DSM 6393 [[Aeromonas ichthiosmia]], DSM 7386, Enteric Group 77, JCM 7375, JCM 8354 [[Aeromonas ichthiosmia]], LMG 12645 [[Aeromonas ichthiosmia]], LMG:12645 [[Aeromonas ichthiosmia]], MTCC 3249 [[Aeromonas culicicola]], NCIMB 13205 [[Aeromonas ichthiosmia]], NICM 5147 [[Aeromonas culicicola]], strain 115/II [[Aeromonas ichthiosmia]]
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