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ABB57047.1 protein (Synechococcus elongatus PCC7942) - STRING interaction network
"ABB57047.1" - annotation not available in Synechococcus elongatus PCC7942
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query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
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proteins of unknown 3D structure
filled nodes:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ABB57047.1annotation not available (253 aa)    
Predicted Functional Partners:
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 (402 aa)
 
      0.782
ABB56689.1
annotation not available (113 aa)
   
          0.593
ABB57048.1
annotation not available (211 aa)
              0.587
ABB57050.1
annotation not available (316 aa)
 
          0.507
aspS
Aspartate--tRNA(Asp/Asn) ligase; 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 (599 aa)
   
   
  0.479
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). Also edits incorrectly charged L-seryl-tRNA(Thr) (604 aa)
 
   
  0.462
nadE
Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source (574 aa)
     
      0.454
ABB57051.1
annotation not available (447 aa)
              0.436
ABB57046.1
annotation not available (160 aa)
              0.433
ABB57049.1
annotation not available (499 aa)
              0.427
Your Current Organism:
Synechococcus elongatus PCC7942
NCBI taxonomy Id: 1140
Other names: Anacystis nidulans R2, S. elongatus PCC 7942, Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC7942, Synechococcus leopoliensis UTEX 2434, Synechococcus leopoliensis strain PCC 7942, Synechococcus sp. IAM M-200, Synechococcus sp. PCC 7942
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