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
-
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
- 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
Advanced search results
Subunits
Subunits on EC 3.6.4.B7 - RadA recombinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
oligomer
polymer
undecamer
additional information
the enzyme forms rings and nucleoprotein filaments. In the presence of ssDNA and ATP-gamma-S helical nucleoprotein filament structures are observed. RadA forms filaments on ssDNA. No protein-DNA complexes are formed on dsDNA. Such preference for binding ssDNA may allow targeting of RadA protein to the ssDNA. In absence of DNA, RadA shows a tendency to form ring-like structures in vivo. Ring structures may be the inactive storage form of the recombinase that are transported to the sites of DNA repair and then converted into functional helical nucleoprotein filaments when loaded onto ssDNA
oligomer
-
Sso RadA proteins are capable of self-assembling into long and fine helical filaments up to 1 lm in length. This unusual protein filament exists not only in solution but also in RadA protein crystals without addition of any nucleotide cofactor. Sso RadA protein filament will dissemble upon incubation with ssDNA substrate and AMP-PNP, and then form only nucleoprotein filaments
the enzyme can selfpolymerize into left-handed helical filaments
polymer
-
the enzyme can selfpolymerize into left-handed helical filaments
-
additional information
RadA has four well-conserved motifs: a potential C4-type zinc-binding motif at the N-terminal domain, a central canonical RecA-like ATPase domain (H1-H4 motifs) and KNRFG motif, and the P/LonC domain at the C-terminus domain
additional information
-
RadA has four well-conserved motifs: a potential C4-type zinc-binding motif at the N-terminal domain, a central canonical RecA-like ATPase domain (H1-H4 motifs) and KNRFG motif, and the P/LonC domain at the C-terminus domain
additional information
-
RadA has four well-conserved motifs: a potential C4-type zinc-binding motif at the N-terminal domain, a central canonical RecA-like ATPase domain (H1-H4 motifs) and KNRFG motif, and the P/LonC domain at the C-terminus domain
-
additional information
RadA is a 460 amino acid protein that has three well-conserved domains also found in other proteins, as well as a 5-amino acid motif highly conserved among radA orthologs. The N-terminal 30 amino acids form a putative zinc-finger domain with a C4 motif, CXXC-Xn-CXXC
additional information
-
RadA is a 460 amino acid protein that has three well-conserved domains also found in other proteins, as well as a 5-amino acid motif highly conserved among radA orthologs. The N-terminal 30 amino acids form a putative zinc-finger domain with a C4 motif, CXXC-Xn-CXXC
additional information
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
additional information
-
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
additional information
-
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
-
additional information
-
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
-
additional information
-
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
-
additional information
-
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
-
additional information
-
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
-
additional information
-
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
-
additional information
-
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
-
additional information
enzyme domain organization, structure comparisons, overview
additional information
enzyme domain organization, structure comparisons, overview
additional information
primary structures of PhoRadA intein, secondary structure based on the determined NMR model. Comparison between the NMR and crystal structures of PhoRadA intein
additional information
-
primary structures of PhoRadA intein, secondary structure based on the determined NMR model. Comparison between the NMR and crystal structures of PhoRadA intein
additional information
highly electrostatic secondary structure elements of the ATPase domain of RadA: helix 1 (D352-K367), loop 1 (R496-R503) and loop 2 (E524-D529)
additional information
-
highly electrostatic secondary structure elements of the ATPase domain of RadA: helix 1 (D352-K367), loop 1 (R496-R503) and loop 2 (E524-D529)
additional information
the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
additional information
-
the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
-
additional information
-
primary structures of PhoRadA intein, secondary structure based on the determined NMR model. Comparison between the NMR and crystal structures of PhoRadA intein
-
additional information
-
the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
-
additional information
-
the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
-
additional information
-
the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
-
additional information
-
the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
-
additional information
-
highly electrostatic secondary structure elements of the ATPase domain of RadA: helix 1 (D352-K367), loop 1 (R496-R503) and loop 2 (E524-D529)
-
additional information
enzyme domain organization, structure comparisons, overview
additional information
-
enzyme domain organization, structure comparisons, overview
-