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
proSProlyl-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 [...] (600 aa)    
Predicted Functional Partners:
ileS
Isoleucyl-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.
  
 0.975
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.
 
 0.934
argS
COG18 Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis].
  
 0.891
leuS
COG495 Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.862
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.
  
 0.855
lysS
COG1190 Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.849
pheT
COG72 Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
 
 0.785
psb27
Possible Photosystem II reaction center Psb27 protein; Plays a role in the repair and/or biogenesis of the calcium- manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of some small extrinsic subunits and thus assembly of calcium-manganese- oxide cluster.
       0.765
uppS
Undecaprenyl pyrophosphate synthetase (UPPS); Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
 
    0.741
aspS
Aspartyl-tRNA synthetase; 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.
  
  
 0.702
Your Current Organism:
Prochlorococcus marinus MIT9301
NCBI taxonomy Id: 167546
Other names: P. marinus str. MIT 9301, Prochlorococcus marinus str. MIT 9301
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