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ProS protein (Rhodobacter sphaeroides 241) - STRING interaction network
"ProS" - Proline--tRNA ligase in Rhodobacter sphaeroides 241
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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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ProSProline--tRNA ligase; 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); Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily (445 aa)    
Predicted Functional Partners:
argS
Arginine--tRNA ligase; IMG reference gene-2512954908; PFAM- DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM- arginyl-tRNA synthetase (580 aa)
   
 
  0.935
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 (984 aa)
     
 
  0.929
leuS
Leucine--tRNA ligase; IMG reference gene-2512955869; PFAM- tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM- leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family (847 aa)
 
 
  0.912
pheT
Phenylalanine--tRNA ligase beta subunit; IMG reference gene-2512953665; PFAM- tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM- phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial (805 aa)
   
 
  0.898
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 (572 aa)
   
 
  0.885
cysS
Cysteine--tRNA ligase; IMG reference gene-2512954667; PFAM- tRNA synthetases class I (C) catalytic domain; TIGRFAM- cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family (499 aa)
 
   
  0.876
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 (987 aa)
     
   
  0.833
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (518 aa)
   
        0.816
serS
Serine--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) (430 aa)
 
 
  0.767
tsaD
tRNA N6-adenosine threonylcarbamoyltransferase; 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 (364 aa)
   
   
  0.764
Your Current Organism:
Rhodobacter sphaeroides 241
NCBI taxonomy Id: 272943
Other names: R. sphaeroides 2.4.1, Rhodobacter sphaeroides 2.4.1, Rhodobacter sphaeroides 241, Rhodobacter sphaeroides ATCC 17023, Rhodobacter sphaeroides ATH 2.4.1, Rhodobacter sphaeroides str. 2.4.1, Rhodobacter sphaeroides strain 2.4.1
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