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
BTN85_1171DNA-directed RNA polymerase subunit M/Transcription elongation factor TFIIS; arCOG00579; gene: RPB9. (98 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.
   
 0.960
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.
   
 0.958
rpoP
DNA-directed RNA polymerase subunit RPC12/RpoP containing C4-type Zn-finger; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoP/eukaryotic RPC10 RNA polymerase subunit family.
   
 0.957
rpoD
DNA-directed RNA polymerase subunit D; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 0.954
rpoN
DNA-directed RNA polymerase subunit 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.
   
 0.954
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.
  
 0.933
tfe
Transcription initiation factor IIE alpha subunit; Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing e [...]
    
 0.923
BTN85_0710
DNA-directed RNA polymerase subunit E'/Rpb7; arCOG00675; gene: RPB7.
   
 0.923
tbp
TATA-box binding protein (TBP), component of TFIID and TFIIIB; General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.
    
 0.922
BTN85_0553
Rad3-related DNA helicase DinG; arCOG00770; gene: dinG.
    
 0.901
Your Current Organism:
Methanohalarchaeum thermophilum
NCBI taxonomy Id: 1903181
Other names: C. Methanohalarchaeum thermophilum, Candidatus Methanohalarchaeum thermophilum, Euryarchaeota archaeon HMET1, archaeon HMET1, strain HMET1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.