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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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from curated databases
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Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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ileSIsoleucyl-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 1 subfamily. (965 aa)    
Predicted Functional Partners:
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 [...]
   
 0.982
argS
Arginyl-tRNA synthetase; Alternative locus ID: PMED4_01931.
  
 0.969
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.
 
 0.968
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.
 
 0.963
leuS
Leucyl-tRNA synthetase; Alternative locus ID: PMED4_10001; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.963
lysS
Lysyl-tRNA synthetase; Alternative locus ID: PMED4_18281; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 0.951
pheT
Phenylalanyl-tRNA synthetase beta chain; Putative assignment; Alternative locus ID: PMED4_09811; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
 
 0.905
prfB
Peptide chain release factor RF-2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
   
  
 0.867
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.
  
 
 0.833
guaA
Glutamine amidotransferase class-I:GMP synthase; Catalyzes the synthesis of GMP from XMP.
   
  
 0.717
Your Current Organism:
Prochlorococcus marinus pastoris
NCBI taxonomy Id: 59919
Other names: P. marinus subsp. pastoris str. CCMP1986, Prochlorococcus marinus MED4, Prochlorococcus marinus subsp. pastoris str. CCMP1378, Prochlorococcus marinus subsp. pastoris str. CCMP1986, Prochlorococcus sp. CCMP1378, Prochlorococcus sp. MED4
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