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Restriction endonuclease BglII Members of this family are predominantly found in prokaryotic restriction endonuclease BglII, and adopt a structure consisting of an alpha/beta core containing a six-stranded beta-sheet surrounded by five alpha-helices, two of which are involved in homodimerization of the endonuclease. They recognize the double-stranded DNA sequence AGATCT and cleave after A-1, resulting in specific double-stranded fragments with terminal 5'-phosphates. |
Lu S et al.(2020). "CDD/SPARCLE: the conserved domain database in 2020.",