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
gidmethylenetetrahydrofolate--tRNA-(uracil(54)- C(5))-methyltransferase (FADH(2)-oxidizing) TrmFO; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily. (437 aa)    
Predicted Functional Partners:
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
 
    0.911
queA
tRNA preQ1(34) S-adenosylmethionine ribosyltransferase-isomerase QueA; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
 
  
 0.794
uppS
Isoprenyl transferase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
  
    0.667
hslU
HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
  
    0.655
hslV
HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
    0.652
udk_2
Uridine kinase; Functions in pyrimidine salvage; pyrimidine ribonucleoside kinase; phosphorylates nucleosides or dinucleosides to make UMP or CMP using ATP or GTP as the donor; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
    0.611
yhbU_2
Protease; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.610
smf
DNA processing protein DprA; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.600
trmD
tRNA (guanosine(37)-N1)-methyltransferase TrmD; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
  
  
 0.590
xerC_4
Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
  
    0.579
Your Current Organism:
Lysinibacillus sphaericus
NCBI taxonomy Id: 1421
Other names: ATCC 14577, B-23268, BCRC 12825, Bacillus sp. G10(2009), Bacillus sphaericus, CCM 2120, CCRC 12825, CCRC:12825, CCUG 7428, CIP 65.30, DSM 28, IAM 13420, JCM 2502, KCTC 3346, L. sphaericus, LMG 7134, LMG:7134, NBRC 15095, NCCB 75018, NCIMB 9370, NCTC 10338, NRRL B-23268, VKM B-509
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