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
tgtQueuine 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 [...] (469 aa)    
Predicted Functional Partners:
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
 
 
    0.909
BF93_03925
glutamyl-Q tRNA(Asp) ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
     0.803
BF93_06940
Membrane protein; Involved in the import of queuosine (Q) precursors, required for Q precursor salvage; Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Q precursor transporter subfamily.
 
     0.792
BF93_08685
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.783
der
Cytidylate kinase; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the cytidylate kinase family. Type 1 subfamily.
  
    0.644
aspS
aspartyl-tRNA synthetase; 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.
 
    0.608
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
   
  
 0.582
ribA
3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate; Belongs to the GTP cyclohydrolase II family.
     
 0.570
BF93_08675
Acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.522
BF93_06655
tRNA/rRNA cytosine-C5-methylase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
  
  
 0.521
Your Current Organism:
Brachybacterium phenoliresistens
NCBI taxonomy Id: 396014
Other names: B. phenoliresistens, BCRC 17589, Brachybacterium phenoliresistens Chou et al. 2007, Brachybacterium sp. phenol-A, JCM 15157, LMG 23707, LMG:23707, strain phenol-A
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