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
dusBtRNA dihydrouridine synthase DusB; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. DusB subfamily. (326 aa)    
Predicted Functional Partners:
OCX46121.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transcriptional regulatory Fis family.
  
  
 0.957
prmA
Hypothetical protein; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.
    
 0.885
accC
acetyl-CoA carboxylase biotin carboxylase subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
 
    0.798
purD
Phosphoribosylamine--glycine ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GARS family.
       0.794
purH
Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.794
rnpA
Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
   
    0.739
trmD
tRNA (guanosine(37)-N1)-methyltransferase TrmD; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
  
  
 0.735
proS
proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...]
   
 
 0.717
panC
Pantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family.
  
    0.699
rpsP
30S ribosomal protein S16; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bS16 family.
   
    0.688
Your Current Organism:
Acidiferrobacter thiooxydans
NCBI taxonomy Id: 163359
Other names: A. thiooxydans, Acidiferrobacter thiooxydans Hallberg et al. 2011, Acidithiobacillus ferrooxidans DSM 2392, DSM 2392, JCM 17358, Thiobacillus ferrooxidans DSM 2392, iron-oxidizing acidophile m-1, strain m-1
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