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
ADI32643.1PFAM: Like-Sm ribonucleoprotein core; SMART: Sm-family ribonucleoprotein. (149 aa)    
Predicted Functional Partners:
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 [...]
   
 0.884
tgtA
tRNA-guanine transglycosylase, various specificities; Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs; Belongs to the archaeosine tRNA-ribosyltransferase family.
       0.870
hel308
DEAD/DEAH box helicase domain protein; DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
   
 0.848
flpA
Fibrillarin; Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA; Belongs to the methyltransferase superfamily. Fibrillarin family.
   
 0.789
ADI32423.1
SMART: RNA polymerase Rbp10.
   
  0.744
rpl7ae
Ribosomal protein L7Ae/L30e/S12e/Gadd45; Multifunctional RNA-binding protein that recognizes the K- turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.
   
  0.729
rpoN
RNA polymerase, N/8 Kd subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoN/eukaryotic RPB10 RNA polymerase subunit family.
  
  0.687
rpoH
RNA polymerase Rpb5; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoH/eukaryotic RPB5 RNA polymerase subunit family.
  
  0.682
ADI32644.1
Hypothetical protein.
       0.655
rpoK
RNA polymerase Rpb6; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoK/eukaryotic RPB6 RNA polymerase subunit family.
   
  0.641
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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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.