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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 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 to each other.
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Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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metGmethionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (632 aa)    
Predicted Functional Partners:
leuS
KEGG: tex:Teth514_0255 leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.994
pheS
KEGG: tex:Teth514_2050 phenylalanyl-tRNA synthetase subunit alpha; TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit; PFAM: phenylalanyl-tRNA synthetase class IIc; aminoacyl tRNA synthetase class II domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
  
 0.991
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 [...]
  
 0.991
argS
TIGRFAM: arginyl-tRNA synthetase; KEGG: tpd:Teth39_0189 arginyl-tRNA synthetase.
  
 0.990
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 1 subfamily.
  
 0.988
lysS
KEGG: tpd:Teth39_0318 lysyl-tRNA synthetase; TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.984
ADH59941.1
KEGG: tpd:Teth39_2136 TatD family hydrolase; TIGRFAM: hydrolase, TatD family; PFAM: TatD-related deoxyribonuclease.
 
 0.976
gltX
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
 
 0.975
gltX-2
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
 
 0.974
pheT
TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: tex:Teth514_2049 phenylalanyl-tRNA synthetase subunit beta.
  
 
 0.973
Your Current Organism:
Thermoanaerobacter mathranii
NCBI taxonomy Id: 583358
Other names: T. mathranii subsp. mathranii str. A3, Thermoanaerobacter mathranii subsp. mathranii A3, Thermoanaerobacter mathranii subsp. mathranii DSM 11426, Thermoanaerobacter mathranii subsp. mathranii str. A3, Thermoanaerobacter mathranii subsp. mathranii strain A3
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