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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
gatCaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. (95 aa)    
Predicted Functional Partners:
gatA
aspartyl/glutamyl-tRNA amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).
 
 0.999
gatB
aspartyl/glutamyl-tRNA amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 
 0.999
ARQ74878.1
Amidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.942
ARQ75070.1
Amidase; Catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.937
aspS
aspartate--tRNA 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.
  
 
 0.931
glnS
glutamine--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.922
ARQ75114.1
Amidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family.
 
 
 0.894
ARQ73514.1
Amidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family.
 
 
 0.891
ARQ75352.1
Amidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.882
rpsN
30S ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
   
    0.711
Your Current Organism:
Pseudomonas fragi
NCBI taxonomy Id: 296
Other names: ATCC 4973, Bacterium fragi, CCUG 556, CFBP 4556, CIP 55.4, DSM 3456, HAMBI 28, IFO 3458, LMG 2191, LMG:2191, NBRC 3458, NCCB 69033, NCIB 8542, NCIB:8542, NCTC 10689, NRRL B-25, NRRL B-727, NRRL:B:25, P. fragi, Pseudomonas fragariae, VKM B-898, VKM:B:898
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