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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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
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experimentally determined
co-expression
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gene co-occurrence
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[Homology]
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serSserine--tRNA ligase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (433 aa)    
Predicted Functional Partners:
selA
L-seryl-tRNA(Sec) selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
    
 0.932
hisS
histidine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.839
yidD
Membrane protein insertion efficiency factor YidD; Could be involved in insertion of integral membrane proteins into the membrane; Belongs to the UPF0161 family.
  
    0.821
cysS
cysteine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.796
valS
valine--tRNA ligase; 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.
 
  
 0.747
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).
  
 
 0.743
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.
 
  
 0.733
tyrS
tyrosine--tRNA ligase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.
 
  
 0.726
gcp
tRNA threonylcarbamoyl adenosine modification protein TsaD; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family.
 
  
 0.721
argS
arginine--tRNA ligase; Catalyzes a two-step reaction, first charging an arginine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class-I aminoacyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.706
Your Current Organism:
Burkholderia cepacia
NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia genomovar I, Burkholderia sp. Bp7081, Burkholderia sp. Bp7091, Burkholderia sp. Bp7098, Burkholderia sp. Bp7108, Burkholderia sp. Bp7432, Burkholderia sp. LK29, Burkholderia sp. NCIM 5465, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717
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