close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
pheS1phenylalanyl-tRNA synthetase, alpha subunit; Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys). (531 aa)    
Predicted Functional Partners:
pscS
Sep-tRNA:Cys-tRNA synthase; Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L- cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)); Belongs to the SepCysS family.
  
 0.998
pheT
phenylalanyl-tRNA synthetase, beta chain.
  
 0.980
serS
seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec); Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily.
 
 
 0.975
valS
valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily.
  
  
 0.920
ADL59152.1
Conserved hypothetical protein.
   
 
 0.879
ribK
Conserved hypothetical protein; Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN); Belongs to the archaeal riboflavin kinase family.
     
 0.868
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).
 
  
 0.772
ribB
Predicted 3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
       0.721
mcrA
Methyl-coenzyme M reductase I, subunit alpha; Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. Neither N-6- mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8- mercaptooctanoylthreonine phosphate (H-SOcoTP) nor any other thiol compound such as CoA or CoM [...]
  
   
 0.720
rpl10e
50S ribosomal protein L10e; Belongs to the universal ribosomal protein uL16 family.
 
 0.706
Your Current Organism:
Methanothermobacter marburgensis
NCBI taxonomy Id: 79929
Other names: M. marburgensis str. Marburg, Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133), Methanobacterium thermoautotrophicum str. Marburg, Methanothermobacter marburgensis str. Marburg, Methanothermobacter marburgensis strain Marburg
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.