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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
trmFOGid protein; 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. (439 aa)    
Predicted Functional Partners:
queA
Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
 
  
 0.789
Mmc1_2541
KEGG: pfo:Pfl_3001 DNA topoisomerase III; TIGRFAM: DNA topoisomerase III; PFAM: TOPRIM domain protein; DNA topoisomerase, type IA, central domain protein; DNA topoisomerase, type IA, Zn finger domain protein; SMART: DNA topoisomerase I, ATP-binding; DNA topoisomerase I, DNA-binding; Toprim sub domain protein.
  
    0.666
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 [...]
  
    0.666
Mmc1_1844
Undecaprenyl pyrophosphate synthetase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
  
    0.657
Mmc1_3483
ATP-dependent DNA helicase, Rep family; PFAM: UvrD/REP helicase; KEGG: rru:Rru_A1536 UvrD/REP helicase.
       0.572
Mmc1_3702
PFAM: methyltransferase small; KEGG: hch:HCH_02224 16S RNA G1207 methylase RsmC; Belongs to the methyltransferase superfamily.
  
    0.569
rlmL
23S rRNA m(2)G-2445 methyltransferase; Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Belongs to the methyltransferase superfamily. RlmKL family.
  
    0.565
proS
prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]
  
    0.552
pyrG
CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
   
    0.517
argS
KEGG: jan:Jann_1507 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase.
   
    0.516
Your Current Organism:
Magnetococcus marinus
NCBI taxonomy Id: 156889
Other names: M. marinus MC-1, Magnetococcus marinus MC-1, Magnetococcus marinus str. MC-1, Magnetococcus marinus strain MC-1, Magnetococcus sp. MC-1
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