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http://purl.uniprot.org/unirules/MF_01125#construct-template-79http://spinrdf.org/sp#subjecthttp://purl.uniprot.org/unirules/MF_01125#construct-var-9
http://purl.uniprot.org/unirules/MF_01125#construct-template-79http://spinrdf.org/sp#predicatehttp://www.w3.org/2000/01/rdf-schema#comment
http://purl.uniprot.org/unirules/MF_01125#construct-template-79http://spinrdf.org/sp#object"Introduction of positive supercoils requires the cooperation of both domains. The helicase-like domain probably does not directly unwind DNA, but more likely acts by driving ATP-dependent conformational changes within the whole enzyme. A beta hairpin in the 'latch' region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and preventing the enzyme from acting as an ATP-independent relaxing enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase domain with the supercoiling activity of the topoisomerase domain."xsd:string
http://purl.uniprot.org/unirules/MF_01125#constructhttps://hamap.expasy.org/rdf/vocab#addsTriplehttp://purl.uniprot.org/unirules/MF_01125#construct-template-79
http://purl.uniprot.org/unirules/MF_01125#construct-template-list-79http://www.w3.org/1999/02/22-rdf-syntax-ns#firsthttp://purl.uniprot.org/unirules/MF_01125#construct-template-79