<http://linkedlifedata.com/resource/#_43334E39423400E> <http://www.w3.org/1999/02/22-rdf-syntax-ns#type> <http://www.w3.org/1999/02/22-rdf-syntax-ns#Statement> .
<http://linkedlifedata.com/resource/#_43334E39423400E> <http://purl.uniprot.org/core/attribution> <http://linkedlifedata.com/resource/#_43334E39423400F> .
<http://linkedlifedata.com/resource/#_43334E39423400E> <http://www.w3.org/1999/02/22-rdf-syntax-ns#subject> <http://purl.uniprot.org/SHA-384/E07F00736B27FBCFBDECC979B107F8BCE271145C3006A8853AC69CE1AE542F7691FBC7AEFEECC429B3AA8017F9DE8DD4> .
<http://linkedlifedata.com/resource/#_43334E39423400E> <http://www.w3.org/1999/02/22-rdf-syntax-ns#predicate> <http://www.w3.org/2000/01/rdf-schema#comment> .
<http://linkedlifedata.com/resource/#_43334E39423400E> <http://www.w3.org/1999/02/22-rdf-syntax-ns#object> "Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated (By similarity)." .