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proS proS ileS ileS argS argS metG metG asnS asnS leuS leuS lysS lysS gltX gltX glnS glnS gluQ gluQ pheT pheT
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[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 [...] (574 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.
   
 0.979
argS
KEGG: aha:AHA_4112 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase.
  
 0.906
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.
  
 0.884
asnS
TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; KEGG: aha:AHA_1486 asparaginyl-tRNA synthetase.
  
 0.863
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: aha:AHA_3247 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.858
lysS
TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; KEGG: aha:AHA_3369 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.838
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).
  
 0.818
glnS
KEGG: eca:ECA1328 glutaminyl-tRNA synthetase; TIGRFAM: glutaminyl-tRNA synthetase; PFAM: glutamyl-tRNA synthetase class Ic.
  
 0.797
gluQ
Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.
  
 0.766
pheT
TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: asa:ASA_1958 phenylalanyl-tRNA synthetase, beta subunit.
  
 
 0.763
Your Current Organism:
Tolumonas auensis
NCBI taxonomy Id: 595494
Other names: T. auensis DSM 9187, Tolumonas auensis DSM 9187, Tolumonas auensis TA 4, Tolumonas auensis str. DSM 9187, Tolumonas auensis strain DSM 9187
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