3.6.4.B7: RadA recombinase
This is an abbreviated version!
For detailed information about RadA recombinase, go to the full flat file.
Word Map on EC 3.6.4.B7
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3.6.4.B7
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strand
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brca2
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single-stranded
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meiotic
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fork
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checkpoint
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reca
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ssdna
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nucleoprotein
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helicase
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stall
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radiosensitivity
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non-homologous
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dna-damaging
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fanconi
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radiation-induced
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chromatid
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mre11
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h2ax
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interstrand
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end-joining
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recombinases
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chk1
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meiosis-specific
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homology-directed
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olaparib
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dna-pkcs
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fancd2
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restart
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prophase
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synaptonemal
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parpis
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error-free
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reca-like
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unrepaired
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gamma-h2ax
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dsb-induced
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d-loops
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ctip
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break-induced
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translesion
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holliday
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bard1
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molecular biology
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synthesis
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atr-dependent
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topbp1
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ssdna-binding
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brca1-mutant
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rucaparib
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diagnostics
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analysis
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pharmacology
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xrcc4
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brca1-deficient
- 3.6.4.B7
- strand
- brca2
-
single-stranded
-
meiotic
- fork
-
checkpoint
- reca
- ssdna
- nucleoprotein
- helicase
-
stall
-
radiosensitivity
-
non-homologous
-
dna-damaging
-
fanconi
-
radiation-induced
-
chromatid
- mre11
- h2ax
-
interstrand
-
end-joining
-
recombinases
- chk1
-
meiosis-specific
-
homology-directed
- olaparib
- dna-pkcs
-
fancd2
-
restart
-
prophase
-
synaptonemal
-
parpis
-
error-free
-
reca-like
-
unrepaired
-
gamma-h2ax
-
dsb-induced
-
d-loops
- ctip
-
break-induced
-
translesion
-
holliday
- bard1
- molecular biology
- synthesis
-
atr-dependent
-
topbp1
-
ssdna-binding
-
brca1-mutant
- rucaparib
- diagnostics
- analysis
- pharmacology
- xrcc4
-
brca1-deficient
Reaction
Synonyms
DNA repair and recombination protein, DNA repair protein RAD51 homolog 1, Hvo RadA, MvRadA, Pho RadA, PhoRadA, Rad51, RadA, RadA intein, RadA recombinase, RadA/Sms, RadC1, RadC2, SMS, SSO0250, SsoRadA, SsoRadA recombinase, SsRada
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.6.4.B7 - RadA recombinase
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proteolytic modification
additional information
the protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation
proteolytic modification
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the protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation
-
proteolytic modification
-
the protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation
-
proteolytic modification
-
the protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation
-
proteolytic modification
-
the protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation
-
proteolytic modification
-
the protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation
-
splicing of the RadA intein located in the ATPase domain of the hyperthermophilic archaeon Pyrococcus horikoshii is strongly regulated by the native exteins, which lock the intein in an inactive state. This splicing trap occurs through interactions between distant residues in the native exteins and the intein, in three-dimensional space. The exteins might thereby serve as an environmental sensor, releasing the intein for full activity only at optimal growth conditions for the native organism, while sparing ATP consumption under conditions of cold-shock. This partnership between the intein and its exteins, which implies co-evolution of the parasitic intein and its host protein may provide another means of post-translational control. Extein-imposed inhibition of splicing can be modulated by solution environment. Post-translational regulation of RadA by superimposed mechanisms, native exteins as sensors that modulate intein splicing
additional information
-
splicing of the RadA intein located in the ATPase domain of the hyperthermophilic archaeon Pyrococcus horikoshii is strongly regulated by the native exteins, which lock the intein in an inactive state. This splicing trap occurs through interactions between distant residues in the native exteins and the intein, in three-dimensional space. The exteins might thereby serve as an environmental sensor, releasing the intein for full activity only at optimal growth conditions for the native organism, while sparing ATP consumption under conditions of cold-shock. This partnership between the intein and its exteins, which implies co-evolution of the parasitic intein and its host protein may provide another means of post-translational control. Extein-imposed inhibition of splicing can be modulated by solution environment. Post-translational regulation of RadA by superimposed mechanisms, native exteins as sensors that modulate intein splicing
additional information
-
splicing of the RadA intein located in the ATPase domain of the hyperthermophilic archaeon Pyrococcus horikoshii is strongly regulated by the native exteins, which lock the intein in an inactive state. This splicing trap occurs through interactions between distant residues in the native exteins and the intein, in three-dimensional space. The exteins might thereby serve as an environmental sensor, releasing the intein for full activity only at optimal growth conditions for the native organism, while sparing ATP consumption under conditions of cold-shock. This partnership between the intein and its exteins, which implies co-evolution of the parasitic intein and its host protein may provide another means of post-translational control. Extein-imposed inhibition of splicing can be modulated by solution environment. Post-translational regulation of RadA by superimposed mechanisms, native exteins as sensors that modulate intein splicing
-