Full Link:
STRINGSTRING
mutM protein (Thermosynechococcus elongatus) - STRING interaction network
"mutM" - formamidopyrimidine-DNA glycosylase in Thermosynechococcus elongatus
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
mutMformamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3’- and 5’-phosphates (By similarity) (284 aa)    
Predicted Functional Partners:
coaE
Hypothetical protein; Catalyzes the phosphorylation of the 3’-hydroxyl group of dephosphocoenzyme A to form coenzyme A (203 aa)
 
   
  0.943
polA
DNA polymerase I (945 aa)
 
   
  0.876
psaE
Photosystem I reaction center subunit IV; Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (76 aa)
         
  0.864
coaD
Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4’- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (168 aa)
   
 
  0.835
recG
ATP-dependent DNA helicase RecG; Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3’- to 5’- polarity. Unwinds branched duplex DNA (Y-DNA) (804 aa)
   
   
  0.812
ruvA
Holliday junction DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB (210 aa)
     
 
  0.722
ruvC
Holliday junction resolvase; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5’-terminal phosphate and a 3’-terminal hydroxyl group (159 aa)
       
 
  0.719
uvrC
Excinuclease ABC subunit C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5’ and 3’ sides of the lesion. The N-terminal half is responsible for the 3’ incision and the C-terminal half is responsible for the 5’ incision (626 aa)
       
 
  0.717
recR
Recombination protein RecR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO (202 aa)
     
 
  0.713
recA
Recombinase A; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (355 aa)
         
  0.711
Your Current Organism:
Thermosynechococcus elongatus
NCBI taxonomy Id: 197221
Other names: T. elongatus, T. elongatus BP-1, Thermosynechococcus, Thermosynechococcus elongatus, Thermosynechococcus elongatus BP-1, Thermosynechococcus elongatus str. BP-1, Thermosynechococcus elongatus strain BP-1
Server load: low (3%) [HD]