close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
miaAtRNA dimethylallyltransferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family. (333 aa)    
Predicted Functional Partners:
miaB
tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
  
 0.982
pheT
phenylalanine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
  
 0.733
AMK57932.1
Cell division protein FtsK; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.697
AMK57930.1
(p)ppGpp synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.694
hflX
GTP-binding protein; GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis.
 
  
 0.684
pgsA
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
     
 0.658
AMK58557.1
DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the LOG family.
     
 0.655
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).
 
      0.639
AMK57934.1
Damage-inducible protein CinA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CinA family.
       0.552
dnaG
DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
 
  
 0.550
Your Current Organism:
Bifidobacterium angulatum
NCBI taxonomy Id: 1683
Other names: AS 1.2265, ATCC 27535, B. angulatum, BCRC 14665, CCRC 14665, CCRC:14665, CCUG 24039, CCUG 24605, CIP 104167, DSM 20098, JCM 7096, LMG 10503, LMG 11039, LMG:10503, LMG:11039, NCFB 2236, NCIMB 702236
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.