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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.6.4.B7
724163
Self-polymerization of archaeal RadA protein into long and fine helical filaments
Biochem. Biophys. Res. Commun.
323
845-851
2004
Saccharolobus solfataricus
15381077
3.6.4.B7
726263
Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein
PLoS One
2
e858
2007
Saccharolobus solfataricus
17848989
3.6.4.B7
723867
Structure of a hexameric form of RadA recombinase from Methanococcus voltae
Acta Crystallogr. Sect. F
68
511-516
2012
Methanococcus voltae
22691778
3.6.4.B7
735255
Sulfolobus tokodaii RadA paralog, stRadC2, is involved in DNA recombination via interaction with RadA and Hjc
Sci. China Life Sci.
55
261-267
2012
Sulfurisphaera tokodaii
22437993
3.6.4.B7
725990
The DNA binding and pairing preferences of the archaeal RadA protein demonstrate a universal characteristic of DNA strand exchange proteins
Mol. Microbiol.
37
555-560
2000
Saccharolobus solfataricus
10931349
3.6.4.B7
725990
The DNA binding and pairing preferences of the archaeal RadA protein demonstrate a universal characteristic of DNA strand exchange proteins
Mol. Microbiol.
37
555-560
2000
Saccharolobus solfataricus P2
10931349
3.6.4.B7
724905
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA-dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75°C
Eur. J. Biochem.
267
1125-1137
2000
Pyrobaculum islandicum
10672022
3.6.4.B7
724905
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA-dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75°C
Eur. J. Biochem.
267
1125-1137
2000
Pyrobaculum islandicum DSM 4184
10672022
3.6.4.B7
725709
The single-stranded DNA binding protein of Sulfolobus solfataricus acts in the presynaptic step of homologous recombination
J. Mol. Biol.
397
31-45
2010
Saccharolobus solfataricus
20080104
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