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recQ protein (Synechocystis sp. PCC6803) - STRING interaction network
"recQ" - ATP-dependent DNA helicase RecQ in Synechocystis sp. PCC6803
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second shell of interactors
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proteins of unknown 3D structure
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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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recQATP-dependent DNA helicase RecQ; DNA helicase (478 aa)    
Predicted Functional Partners:
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3’ to 5’ and 5’ to 3’ exonuclease activity (986 aa)
   
  0.987
sbcD
Hypothetical 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 (416 aa)
   
  0.979
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 (354 aa)
     
  0.978
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA super [...] (898 aa)
   
  0.960
uvrD
DNA helicase II (793 aa)
   
 
  0.943
sbcC
Hypothetical 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 (1006 aa)
   
  0.905
sll1121
Hypothetical protein (770 aa)
   
 
  0.905
recJ
single-strand-DNA-specific exonuclease (759 aa)
 
   
  0.884
crhR
ATP-dependent RNA helicase DeaD; An ATP-dependent bidirectional RNA helicase with RNA- dependent ATPase activity; does not unwind dsDNA, uses only (d)ATP (PubMed-15542859). Also has ATP-dependent RNA annealing activity; concurrent annealing and helicase activity promote strand-exchange activity (PubMed-15542859). In vitro has low helicase processivity, annealing processivity is probably higher (PubMed-15542859). Required for correct cold adaptation, probably by aiding translation of mRNAs required for photosynthesis and electron transport (PubMed-22575444). Probably regulates the cold- [...] (492 aa)
 
0.881
sll1366
Helicase of the snf2/rad54 family (1039 aa)
   
 
  0.857
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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