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
rpoA2DNA-directed RNA polymerase, subunit A'; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (516 aa)    
Predicted Functional Partners:
rpoK
DNA-directed RNA polymerase, subunit K/omega; 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.
 
 0.999
AGB04369.1
PFAM: S1 RNA binding domain; RNA polymerase Rpb7-like, N-terminal domain; TIGRFAM: DNA-directed RNA polymerase (rpoE), archaeal and eukaryotic form.
   
 0.999
AGB05257.1
DNA-directed RNA polymerase subunit A; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 0.999
AGB05258.1
DNA-directed RNA polymerase subunit B; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
 0.999
rpoH
DNA-directed RNA polymerase, subunit H, RpoH/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.
 
 0.999
rpoD
DNA-directed RNA polymerase, alpha subunit/40 kD subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoD/eukaryotic RPB3 RNA polymerase subunit family.
 
 0.997
rpoN
DNA-directed RNA polymerase, subunit N (RpoN/RPB10); 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.
  
 0.995
rpoL
DNA-directed RNA polymerase, subunit L; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoL/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
  
 0.990
nusA
NusA family KH domain protein; Participates in transcription termination. Belongs to the NusA family.
 
 
 0.962
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 [...]
 
 0.936
Your Current Organism:
Aciduliprofundum sp. MAR08339
NCBI taxonomy Id: 673860
Other names: A. sp. MAR08-339, Aciduliprofundum sp. MAR08-339
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.