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STRINGSTRING
rgy protein (Thermoproteus tenax) - STRING interaction network
"rgy" - Reverse gyrase in Thermoproteus tenax
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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rgyReverse gyrase; Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5’ DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication; In the C-terminal section; belongs to the prokaryotic type I/III topoisomerase family (1223 aa)    
Predicted Functional Partners:
pyrE
Orotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) (193 aa)
           
  0.948
speE
Polyamine aminopropyltransferase; Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy- AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine; Belongs to the spermidine/spermine synthase family (288 aa)
         
  0.903
radA
DNA repair and recombination protein RadA; Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (382 aa)
           
  0.898
thyX
Flavin-dependent thymidylate synthase; Catalyzes the reductive methylation of 2’-deoxyuridine- 5’-monophosphate (dUMP) to 2’-deoxythymidine-5’-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant (244 aa)
           
  0.891
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 (893 aa)
   
     
  0.835
TTX_1870
Nucleoside-triphosphatase TTX_1870; Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency (166 aa)
   
     
  0.814
mvk
Mevalonate kinase; Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids; Belongs to the GHMP kinase family. Mevalonate kinase subfamily (314 aa)
           
  0.807
hjr
Holliday junction resolvase Hjc; A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5’-terminal phosphate and a 3’-terminal hydroxyl group that are ligated to produce recombinant products; Belongs to the Holliday junction resolvase Hjc family (135 aa)
           
  0.794
tfs/rpoM
annotation not available (109 aa)
           
  0.785
tfe
Transcription factor E; 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 elongation complexes. Seems [...] (178 aa)
 
     
  0.714
Your Current Organism:
Thermoproteus tenax
NCBI taxonomy Id: 768679
Other names: T. tenax Kra 1, Thermoproteus tenax, Thermoproteus tenax DSM 2078, Thermoproteus tenax JCM 9277, Thermoproteus tenax Kra 1, Thermoproteus tenax str. Kra 1, Thermoproteus tenax strain Kra 1
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