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
tsaEATP-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (161 aa)    
Predicted Functional Partners:
tsaB
Peptidase M22; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.981
CN97_13600
Aminoglycoside phosphotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
      0.965
tsaD
Protein kinase; 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.
 
 
 0.938
CN97_13605
Nucleotidyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
      0.867
nnrE
Hypothetical 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 dehydratase to allow the repair of both epi [...]
  
 
 0.808
CN97_12530
Translation factor Sua5; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
 
  
 0.775
addA
Helicase UvrD; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the helicase family. UvrD subfamily.
 
   
 0.747
CN97_13610
Helicase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.745
ispDF
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D- erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4- diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C- methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
     
 0.631
trxA
Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family.
       0.618
Your Current Organism:
Haematobacter massiliensis
NCBI taxonomy Id: 195105
Other names: CCUG 47968, CIP 107725, H. massiliensis, Haematobacter massiliensis Heisel et al. 2007, Rhodobacter massiliensis, Rhodobacter massiliensis Greub and Raoult 2006, cf. Rhodobacter sp. Framboise, strain Framboise
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.