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Mettu_1449 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1449" - PFAM: Glutathione S-transferase, N-terminal in Methylobacter tundripaludum
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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 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]
Score
Mettu_1449PFAM- Glutathione S-transferase, N-terminal; KEGG- mca-MCA1002 glutathione S-transferase domain-containing protein (215 aa)    
Predicted Functional Partners:
gshB
PFAM- Prokaryotic glutathione synthetase, ATP-binding; Prokaryotic glutathione synthetase, N-terminal; TIGRFAM- Glutathione synthetase, prokaryotic; HAMAP- Glutathione synthetase, prokaryotic; KEGG- mca-MCA2338 glutathione synthetase; Belongs to the prokaryotic GSH synthase family (315 aa)
       
  0.803
Mettu_3056
Gamma-glutamyltransferase; TIGRFAM- Gamma-glutamyltranspeptidase; KEGG- mca-MCA2148 gamma-glutamyltranspeptidase; PFAM- Gamma-glutamyltranspeptidase (557 aa)
         
  0.783
Mettu_4379
TIGRFAM- Glutathione reductase, plant; KEGG- nhl-Nhal_3170 glutathione-disulfide reductase; PFAM- FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family (449 aa)
     
 
  0.781
Mettu_3996
PFAM- Glutathione S-transferase, C-terminal; Glutathione S-transferase, N-terminal; KEGG- lbf-LBF_2202 glutathione transferase (201 aa)
   
   
    0.707
rplR
50S ribosomal protein L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance (117 aa)
     
    0.678
lysS
Lysine--tRNA ligase; PFAM- Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; TIGRFAM- Lysyl-tRNA synthetase, class II; HAMAP- Lysyl-tRNA synthetase; KEGG- nhl-Nhal_2437 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family (499 aa)
     
  0.670
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (528 aa)
     
 
  0.662
metG
Methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily (672 aa)
     
  0.662
proS
Proline--tRNA ligase; 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 deacy [...] (569 aa)
     
    0.639
rpsB
KEGG- mca-MCA0567 30S ribosomal protein S2; TIGRFAM- Ribosomal protein S2, bacteria/mitochondria/plastid; PFAM- Ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family (245 aa)
     
        0.619
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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