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
hisSTIGRFAM: histidyl-tRNA synthetase; KEGG: rak:A1C_02295 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family. (429 aa)    
Predicted Functional Partners:
eif2a
Translation initiation factor 2, alpha subunit; eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. Belongs to the eIF-2-alpha family.
   
 0.904
ADI32562.1
PFAM: tRNA intron endonuclease, catalytic domain protein; tRNA intron endonuclease domain protein.
       0.870
eif2g
Protein synthesis factor GTP-binding protein; eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.
  
 0.845
thrS
KEGG: dvl:Dvul_0707 threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; PFAM: Threonyl-tRNA synthetase editing domain protein; Anticodon-binding domain protein; tRNA synthetase class II (G H P and S); Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.798
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
  
 0.786
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).
 
 
 0.719
cysS
KEGG: sfu:Sfum_1634 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: Cysteinyl-tRNA synthetase class Ia; tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia DALR.
 
  
 0.694
ADI31202.1
aminoacyl-tRNA synthetase class Ia; KEGG: rbe:RBE_0509 valyl-tRNA synthetase.
 
 
 0.692
fusA
Translation elongation factor aEF-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; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF [...]
 
 
 0.689
alaS
alanyl-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.
 
 
 0.685
Your Current Organism:
Staphylothermus hellenicus
NCBI taxonomy Id: 591019
Other names: S. hellenicus DSM 12710, Staphylothermus hellenicus BK20S6-10-b1, Staphylothermus hellenicus DSM 12710, Staphylothermus hellenicus P8, Staphylothermus hellenicus str. DSM 12710, Staphylothermus hellenicus strain DSM 12710, Staphylothermus sp. P8
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