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
tgttRNA guanosine(34) transglycosylase Tgt; 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 t [...] (406 aa)    
Predicted Functional Partners:
OGZ04434.1
Thymidylate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
    0.919
OGZ04752.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
       0.664
OGZ04432.1
Deoxyuridine 5'-triphosphate nucleotidohydrolase; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
    
  0.656
OGZ03749.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
    0.587
OGZ04435.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
    
  0.572
OGZ04754.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
       0.556
hisS
histidine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.513
OGZ04448.1
50S ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
  
    0.496
aspS
Hypothetical protein; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
    0.468
smpB
SsrA-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to [...]
   
   0.466
Your Current Organism:
Lloydbacteria bacterium RIFCSPHIGHO201FULL4120
NCBI taxonomy Id: 1798657
Other names: C. Lloydbacteria bacterium RIFCSPHIGHO2_01_FULL_41_20, Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_01_FULL_41_20
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