• Version:
  • 11.0 (preview - - version 10.5 still available here)
STRINGSTRING
cysS protein (Methanococcus voltae) - STRING interaction network
"cysS" - Cysteine--tRNA ligase in Methanococcus voltae
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
cysSCysteine--tRNA ligase; TIGRFAM- cysteinyl-tRNA synthetase; KEGG- gme-Gmet_0057 cysteinyl-tRNA synthetase; PFAM- Cysteinyl-tRNA synthetase class Ia; Cysteinyl-tRNA synthetase class Ia DALR; tRNA synthetase class I (M) (559 aa)    
Predicted Functional Partners:
leuS
Leucine--tRNA ligase; KEGG- similar to leucyl-tRNA synthetase; K01869 leucyl-tRNA synthetase; TIGRFAM- leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family (1000 aa)
 
 
  0.974
ileS
Isoleucine--tRNA ligase; 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 (1053 aa)
 
   
  0.964
Mvol_0651
O-phospho-L-seryl-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 (399 aa)
         
  0.961
thrS
Threonine--tRNA ligase; KEGG- gbm-Gbem_1990 threonyl-tRNA synthetase; TIGRFAM- threonyl-tRNA synthetase; PFAM- Threonyl-tRNA synthetase editing domain protein; tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family (629 aa)
 
   
  0.940
valS
Valine--tRNA ligase; 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 (907 aa)
 
   
  0.937
gltX
Glutamate--tRNA ligase; 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) (574 aa)
 
   
  0.883
tuf
Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (428 aa)
   
 
  0.858
fusA
Elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (727 aa)
 
   
  0.834
argS
Arginine--tRNA ligase; TIGRFAM- arginyl-tRNA synthetase; KEGG- rma-Rmag_0079 arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family (590 aa)
   
 
  0.807
alaS
Alanine--tRNA ligase; 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 (936 aa)
 
   
  0.784
Your Current Organism:
Methanococcus voltae
NCBI taxonomy Id: 456320
Other names: M. voltae A3, Methanococcus voltae, Methanococcus voltae A3, Methanococcus voltae str. A3, Methanococcus voltae strain A3
Server load: low (11%) [HD]