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mutS protein (Nitrosomonas eutropha) - STRING interaction network
"mutS" - DNA mismatch repair protein MutS in Nitrosomonas eutropha
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
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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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 each other.
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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mutSDNA mismatch repair protein MutS; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity (880 aa)    
Predicted Functional Partners:
mutL
DNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (608 aa)
 
  0.955
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (906 aa)
   
 
  0.841
Neut_0002
Beta sliding clamp; 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 as [...] (373 aa)
     
 
  0.601
Neut_2545
PFAM- UvrD/REP helicase; KEGG- fnu-FN0524 DNA helicase II; Belongs to the helicase family. UvrD subfamily (971 aa)
   
 
  0.573
gyrB
DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner (809 aa)
   
 
  0.538
priA
Primosomal protein N’; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA (733 aa)
 
        0.531
Neut_2523
TIGRFAM- ATP-dependent DNA helicase, RecQ family; ATP-dependent DNA helicase RecQ; PFAM- helicase domain protein; DEAD/DEAH box helicase domain protein; KEGG- neu-NE2564 ATP-dependent DNA helicase RecQ (539 aa)
   
 
  0.527
Neut_2467
Vitamin B12-dependent ribonucleotide reductase; Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen (957 aa)
     
      0.520
Neut_0773
PFAM- UvrD/REP helicase; KEGG- neu-NE1473 UvrD/REP helicase (748 aa)
     
 
  0.512
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 (863 aa)
   
 
  0.504
Your Current Organism:
Nitrosomonas eutropha
NCBI taxonomy Id: 335283
Other names: N. eutropha C91, Nitrosomonas eutropha, Nitrosomonas eutropha C91, Nitrosomonas eutropha str. C91, Nitrosomonas eutropha strain C91
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