STRINGSTRING
mutT protein (Synechocystis sp. PCC6803) - STRING interaction network
"mutT" - Mutator MutT protein in Synechocystis sp. PCC6803
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query proteins and first shell of interactors
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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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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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Gene Fusion
Cooccurence
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Experiments
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[Homology]
Score
mutTMutator MutT protein (136 aa)    
Predicted Functional Partners:
nnr
Hypothetical protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity) (524 aa)
   
  0.959
pyrG
CTP synthetase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (552 aa)
   
 
  0.766
slr1690
Hypothetical protein (261 aa)
         
  0.751
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3’ to 5’ and 5’ to 3’ exonuclease activity (986 aa)
   
 
  0.750
recN
DNA repair protein; May be involved in recombinational repair of damaged DNA (584 aa)
     
 
  0.746
zam
Protein conferring resistance to acetazolamide; Not known; control resistance to the carbonic anhydrase inhibitor acetazolamide (781 aa)
   
  0.739
sll1290
Ribonuclease II (666 aa)
   
  0.739
nrdA
Ribonucleotide reductase subunit alpha; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity) (767 aa)
   
  0.733
SYNGTS_1584
polyA polymerase (942 aa)
   
   
  0.718
mutM
formamidopyrimidine-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) (287 aa)
       
 
  0.697
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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