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.
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
alaSAlanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. (892 aa)    
Predicted Functional Partners:
leuS
Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.988
ileS
Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
  
 
 0.981
htpX
Peptidase family M48; Belongs to the peptidase M48B family.
  
  
 0.958
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.
 
  
 0.947
MMP0398
Conserved hypothetical archaeal protein.
  
    0.945
ehbQ
Conserved hypothetical protein; Citation: Tersteegen, A. and R. Hedderich. 1999. Eur. J. Biochem. 264:930-43. Curr. Opin. Struct. Biol. 2001; 11:694-700.
  
    0.930
thrS
Threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.925
argS
Arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.903
aspC
Aspartate aminotransferase; Citation: Tanaka T, Yamamoto S, Moriya T, Taniguchi M, Hayashi H, Kagamiyama H, Oi S. (1994) J Biochem (Tokyo) 115:309-17.
  
  
 0.895
secD
SecD/SecF/SecDF export membrane protein; Involved in protein export.
  
  
 0.887
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
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