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
polAUnannotated protein; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. (880 aa)    
Predicted Functional Partners:
GCA_000797495_01090
Unannotated protein.
  
 0.999
asnS_2
Unannotated protein.
  
 0.999
sbcD
Unannotated protein; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family.
  
 0.999
sbcC
Unannotated protein.
  
 0.999
asnS_1
Unannotated protein; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
  
 0.999
dnaN
Unannotated protein; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication [...]
 
 0.999
yhaO
Unannotated protein.
  
 0.999
exoA
Unannotated protein.
  
 0.999
recQ
Unannotated protein.
  
 0.995
mutM
Unannotated protein.
  
  
 0.985
Your Current Organism:
Robinsoniella peoriensis
NCBI taxonomy Id: 180332
Other names: CCUG 48729, Clostridium sp. CCUG 52336, NRRL B-23985, R. peoriensis, Robinsoniella peoriensis Cotta et al. 2009, strain PPC31, swine fecal bacterium FPC47, swine fecal bacterium FPC50, swine manure pit bacterium PPC108, swine manure pit bacterium PPC31, swine manure pit bacterium PPC37, swine manure pit bacterium PPC44
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.