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
ACZ22950.1PFAM: tRNA synthetases class I (M); TIGRFAM: methionyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (536 aa)    
Predicted Functional Partners:
leuS
leucyl-tRNA synthetase; PFAM: Anticodon-binding domain; tRNA synthetases class I (M); TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; glutamate--cysteine ligase/gamma-glutamylcysteine synthetase, Streptococcus agalactiae type; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.921
metG
methionyl-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.
  
  
 
0.918
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.
  
 0.913
ACZ21536.1
Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
  
 
 0.912
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
     
 0.912
metE
Methionine synthase (B12-independent); Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family.
     
 0.900
ACZ23603.1
Methionine synthase II (cobalamin-independent).
     
 0.900
argS
PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase.
 
 0.861
pheT
phenylalanyl-tRNA synthetase beta subunit; PFAM: Putative tRNA binding domain; Ferredoxin-fold anticodon binding domain; B3/4 domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.859
proS
prolyl-tRNA synthetase, family II; 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 i [...]
  
 0.819
Your Current Organism:
Sanguibacter keddieii
NCBI taxonomy Id: 446469
Other names: S. keddieii DSM 10542, Sanguibacter keddieii DSM 10542, Sanguibacter keddieii str. DSM 10542, Sanguibacter keddieii strain DSM 10542
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