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
Ccel_0365PFAM: ATP dependent DNA ligase; KEGG: nth:Nther_0138 ATP dependent DNA ligase. (324 aa)    
Predicted Functional Partners:
Ccel_0366
TIGRFAM: DNA polymerase LigD, polymerase domain protein; PFAM: DNA primase small subunit; KEGG: swo:Swol_1124 hypothetical protein.
  
 0.999
ku
Ku protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family.
 
  
 0.987
Ccel_0002
DNA polymerase III, beta subunit; 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 [...]
   
 0.981
Ccel_3322
TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: cth:Cthe_0458 exodeoxyribonuclease III Xth.
  
 
 0.942
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
  
 0.892
Ccel_0363
TIGRFAM: regulatory protein, FmdB family; PFAM: Putative regulatory protein FmdB; KEGG: cth:Cthe_1941 FmdB family regulatory protein.
       0.543
Ccel_0367
TIGRFAM: UDP-glucose 4-epimerase; PFAM: NAD-dependent epimerase/dehydratase; short-chain dehydrogenase/reductase SDR; 3-beta hydroxysteroid dehydrogenase/isomerase; polysaccharide biosynthesis protein CapD; dTDP-4-dehydrorhamnose reductase; Male sterility domain; KEGG: drm:Dred_3002 UDP-glucose 4-epimerase; Belongs to the NAD(P)-dependent epimerase/dehydratase family.
       0.536
ligA
DNA ligase, NAD-dependent; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
     
 0.526
Ccel_1759
PFAM: beta-lactamase domain protein; RNA-metabolising metallo-beta-lactamase; KEGG: cth:Cthe_0611 RNA-metabolising metallo-beta-lactamase.
  
 0.476
tpiA
Phosphoglycerate kinase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family.
     
 0.465
Your Current Organism:
Ruminiclostridium cellulolyticum
NCBI taxonomy Id: 394503
Other names: Clostridium cellulolyticum H10, R. cellulolyticum H10, Ruminiclostridium cellulolyticum H10
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.