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
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[Homology]
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queAS-adenosylmethionine/tRNA-ribosyltransferase- isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). (361 aa)    
Predicted Functional Partners:
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...]
 
 
 0.992
ruvB
Holliday junction DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
 
  
 0.823
Msil_3682
TIGRFAM: iron-sulfur cluster binding protein; PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; domain of unknown function DUF1730; KEGG: bid:Bind_3314 iron-sulfur cluster binding protein.
 
  
 0.823
Msil_3556
PFAM: Glutathione S-transferase domain; KEGG: bur:Bcep18194_C7686 glutathione S-transferase-like protein; Belongs to the GST superfamily.
       0.773
Msil_1956
KEGG: rpb:RPB_3475 hypothetical protein.
  
  
 0.740
queF
7-cyano-7-deazaguanine reductase; Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily.
 
  
 0.676
Msil_3553
Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
       0.654
ruvA
Holliday junction DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
  
  
 0.614
Msil_1117
PFAM: TPR repeat-containing protein; Tetratricopeptide TPR_2 repeat protein; SMART: Tetratricopeptide domain protein; KEGG: bid:Bind_0857 tetratricopeptide TPR_2 repeat protein.
  
    0.562
queC
exsB protein; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family.
 
   
 0.529
Your Current Organism:
Methylocella silvestris
NCBI taxonomy Id: 395965
Other names: M. silvestris BL2, Methylocella silvestris BL2, Methylocella silvestris str. BL2, Methylocella silvestris strain BL2, Methylocella sp. BL2
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