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Acin_1192 protein (Acidaminococcus intestini) - STRING interaction network
"Acin_1192" - Peptidase M24 in Acidaminococcus intestini
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Acin_1192Peptidase M24 (350 aa)    
Predicted Functional Partners:
Acin_1191
Translation elongation factor P (185 aa)
   
 
  0.866
Acin_1194
Aminodeoxychorismate lyase (338 aa)
              0.710
Acin_1196
Hypothetical protein; Could be a nuclease involved in processing of the 5’-end of pre-16S rRNA (135 aa)
              0.699
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 (885 aa)
 
   
  0.692
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA super [...] (754 aa)
   
   
  0.688
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (874 aa)
   
   
  0.669
map
Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (272 aa)
   
   
  0.652
hisS
histidyl-tRNA synthetase (428 aa)
 
   
  0.626
Acin_1185
Zinc-dependent peptidase (973 aa)
   
      0.605
polA
DNA polymerase I (873 aa)
   
   
  0.602
Your Current Organism:
Acidaminococcus intestini
NCBI taxonomy Id: 568816
Other names: A. intestini, A. intestini RyC-MR95, Acidaminococcus intestini, Acidaminococcus intestini Jumas-Bilak et al. 2007, Acidaminococcus intestini RyC-MR95, Acidaminococcus intestini strain RyC-MR95, Acidaminococcus sp. ADV 255.99
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