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GCWU000321_00449 protein (Dialister invisus) - STRING interaction network
"GCWU000321_00449" - Ser/Thr phosphatase family protein in Dialister invisus
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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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[Homology]
Score
GCWU000321_00449Ser/Thr phosphatase family protein (421 aa)    
Predicted Functional Partners:
GCWU000321_00448
Uncharacterized protein (997 aa)
 
 
 
  0.987
sbcC
Nuclease SbcCD subunit C ; 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 (880 aa)
   
  0.986
polA
DNA polymerase (858 aa)
   
  0.983
recQ
ATP-dependent DNA helicase RecQ (811 aa)
 
  0.909
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 (356 aa)
   
  0.896
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 supe [...] (799 aa)
   
  0.822
GCWU000321_01606
Metallo-beta-lactamase domain protein (361 aa)
     
  0.769
dnaN
DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA (369 aa)
   
  0.768
GCWU000321_01367
SNF2 family N-terminal domain protein (459 aa)
   
 
  0.680
dinB
DNA polymerase IV ; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3’-5’ exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (403 aa)
 
 
  0.597
Your Current Organism:
Dialister invisus
NCBI taxonomy Id: 592028
Other names: D. invisus, D. invisus DSM 15470, Dialister invisus, Dialister invisus DSM 15470, Dialister invisus Downes et al. 2003, Dialister invisus str. DSM 15470, Dialister invisus strain DSM 15470
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