STRINGSTRING
STRING protein interaction network
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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AGA91735.1NTP pyrophosphohydrolase; PFAM: NUDIX domain. (162 aa)    
Predicted Functional Partners:
AGA91662.1
PFAM: 6-pyruvoyl tetrahydropterin synthase.
 
  
  0.913
folE2
Hypothetical protein; Converts GTP to 7,8-dihydroneopterin triphosphate.
  
  
  0.912
folE
PFAM: GTP cyclohydrolase I; TIGRFAM: GTP cyclohydrolase I.
    
  0.909
nnrE
yjeF-like protein, hydroxyethylthiazole kinase-related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate d [...]
  
 0.906
aspS
aspartyl-tRNA synthetase; 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.
  
   0.902
AGA89913.1
PFAM: Alkaline phosphatase; Belongs to the alkaline phosphatase family.
     
 0.900
birA
birA, biotin-(acetyl-CoA-carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
   
    0.612
AGA91656.1
PFAM: NlpB/DapX lipoprotein.
  
     0.596
AGA90161.1
PFAM: CNP1-like family.
 
     0.564
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
     
 0.557
Your Current Organism:
Thioflavicoccus mobilis
NCBI taxonomy Id: 765912
Other names: T. mobilis 8321, Thioflavicoccus mobilis 8321, Thioflavicoccus mobilis ATCC 700959, Thioflavicoccus mobilis str. 8321, Thioflavicoccus mobilis strain 8321
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.