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
dnaGDNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. (596 aa)    
Predicted Functional Partners:
AEM80013.1
Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily.
 0.950
sigA
RNA polymerase, sigma 70 subunit, RpoD subfamily; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
 
  
 0.942
AEM79508.1
TOPRIM domain-containing protein; KEGG: chy:CHY_2640 DNA primase, internal deletion; PFAM: Toprim domain; DNA primase, catalytic core, N-terminal; SMART: Toprim domain, subgroup.
     
 
0.900
polA
5'-3' exonuclease, resolvase-like domain-containing protein; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
 
  
 0.815
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
    
 
 0.724
AEM79083.1
Deoxyguanosinetriphosphate triphosphohydrolase-like protein; SMART: Metal-dependent phosphohydrolase, HD region; TIGRFAM: Deoxyguanosinetriphosphate triphosphohydrolase; KEGG: tbo:Thebr_0759 deoxyguanosinetriphosphate triphosphohydrolase; HAMAP: Deoxyguanosinetriphosphate triphosphohydrolase-like protein; PFAM: Metal-dependent phosphohydrolase, HD region, subdomain; Belongs to the dGTPase family. Type 2 subfamily.
     
 0.686
trmD
tRNA (guanine-N(1)-)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
 
  
 0.668
AEM79180.1
TIGRFAM: DNA polymerase III, alpha subunit; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; Nucleic acid binding, OB-fold, tRNA/helicase-type; KEGG: tbo:Thebr_0699 DNA polymerase III subunit alpha; SMART: Polymerase/histidinol phosphatase, N-terminal.
 
  
 0.660
der
GTP-binding protein engA; GTPase that plays an essential role in the late steps of ribosome biogenesis; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
  
  
 0.629
AEM79799.1
TIGRFAM: Small GTP-binding protein; PFAM: GTP-binding protein, HSR1-related; KEGG: tit:Thit_2142 small GTP-binding protein; SMART: Ras small GTPase, Ras type.
  
  
 0.629
Your Current Organism:
Thermoanaerobacter wiegelii
NCBI taxonomy Id: 697303
Other names: T. wiegelii Rt8.B1, Thermoanaerobacter wiegelii Rt8.B1, Thermoanaerobacter wiegelii str. Rt8.B1, Thermoanaerobacter wiegelii strain Rt8.B1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.