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Literature summary extracted from

  • Raymond, A.; Shuman, S.
    Deinococcus radiodurans RNA ligase exemplifies a novel ligase clade with a distinctive N-terminal module that is important for 5-PO4 nick sealing and ligase adenylylation but dispensable for phosphodiester formation at an adenylylated nick (2007), Nucleic Acids Res., 35, 839-849.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
6.5.1.3 E230A mutant is defective in phosphodiester formation at a preadenylylated nick Deinococcus radiodurans
6.5.1.3 E230A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
6.5.1.3 E230D mutation reduces nick sealing activity to 1% of the wild-type level Deinococcus radiodurans
6.5.1.3 E230Q mutation reduces nick sealing activity to less than 1% of the wild-type level Deinococcus radiodurans
6.5.1.3 E305A mutant is defective in phosphodiester formation at a preadenylylated nick Deinococcus radiodurans
6.5.1.3 E305A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
6.5.1.3 E305D mutation reduces nick sealing activity to 1% of the wild-type level Deinococcus radiodurans
6.5.1.3 E305Q mutation reduces nick sealing activity to 7% of the wild-type level Deinococcus radiodurans
6.5.1.3 F281A mutant is defective in phosphodiester formation at a preadenylylated nick Deinococcus radiodurans
6.5.1.3 F281A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
6.5.1.3 F281L mutation reduces nick sealing activity to 5% of the wild-type level Deinococcus radiodurans
6.5.1.3 G168A mutant is defective in phosphodiester formation at a preadenylylated nick Deinococcus radiodurans
6.5.1.3 G168A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
6.5.1.3 H167A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
6.5.1.3 H167N mutation reduces nick sealing activity to 7% of the wild-type level Deinococcus radiodurans
6.5.1.3 H167Q mutation reduces nick sealing activity to less than 1% of the wild-type level Deinococcus radiodurans
6.5.1.3 K186A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
6.5.1.3 K186Q mutation reduces nick sealing activity to 1% of the wild-type level Deinococcus radiodurans
6.5.1.3 K186R mutation reduces nick sealing activity to 3% of the wild-type level Deinococcus radiodurans
6.5.1.3 K326Q mutation reduces nick sealing activity to less than 1% of the wild-type level Deinococcus radiodurans
6.5.1.3 K326R mutation reduces nick sealing activity to 3% of the wild-type level Deinococcus radiodurans
6.5.1.3 S185N mutation reduces nick sealing activity to less than 1% of the wild-type level Deinococcus radiodurans
6.5.1.3 S185T mutation reduces nick sealing activity to 12% of the wild-type level Deinococcus radiodurans
6.5.1.3 T163A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
6.5.1.3 T163S mutation reduces nick sealing activity to 2% of the wild-type level Deinococcus radiodurans
6.5.1.3 T163V mutation reduces nick sealing activity to 30% of the wild-type level Deinococcus radiodurans

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.3 Deinococcus radiodurans
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Synonyms

EC Number Synonyms Comment Organism
6.5.1.3 DraRnl
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 Deinococcus radiodurans