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
Ajs_0924PFAM: protein phosphatase 2C domain protein; Stage II sporulation E family protein; KEGG: pol:Bpro_1338 protein serine/threonine phosphatases. (300 aa)    
Predicted Functional Partners:
Ajs_0925
PFAM: protein kinase; SMART: tyrosine protein kinase; serine/threonine protein kinase; KEGG: pol:Bpro_1337 serine/threonine protein kinase.
 
 
 0.973
Ajs_0624
PFAM: protein kinase; SMART: tyrosine protein kinase; serine/threonine protein kinase; KEGG: bte:BTH_II0256 serine/threonine protein kinase.
 
 
 0.881
Ajs_4043
PFAM: Forkhead-associated protein; KEGG: pol:Bpro_4677 FHA domain containing protein.
 
 
 0.789
Ajs_2096
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: biotin/lipoyl attachment domain-containing protein; FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glucose-inhibited division protein A; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: rfr:Rfer_2214 dihydrolipoamide dehydrogenase.
  
 0.775
Ajs_2123
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: biotin/lipoyl attachment domain-containing protein; FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glucose-inhibited division protein A; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: rfr:Rfer_2214 dihydrolipoamide dehydrogenase.
  
 0.775
rph
RNAse 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.
     
 0.745
Ajs_0480
PFAM: protein kinase; UspA domain protein; SMART: tyrosine protein kinase; serine/threonine protein kinase; KEGG: ade:Adeh_3699 serine/threonine protein kinase.
 
 
 0.744
Ajs_0926
PFAM: YicC N-terminal domain protein; domain of unknown function DUF1732; KEGG: rfr:Rfer_1626 conserved hypothetical protein 255.
       0.731
Ajs_0922
Non-canonical purine NTP pyrophosphatase, rdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
   
   0.706
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
  
   0.701
Your Current Organism:
Acidovorax sp. JS42
NCBI taxonomy Id: 232721
Other names: A. sp. JS42
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