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The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. 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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"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01125"}],"value":"This enzyme is the only unique feature of hyperthermophilic bacteria/archaea known and seems to be essential for adaptation to life at high temperatures. It may play a role in stabilization of DNA at high temperatures"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01383"}],"value":"Belongs to the type IA topoisomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01125"}],"value":"In the C-terminal section; belongs to the type IA topoisomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043976"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01125"}],"value":"In the N-terminal section; belongs to the DEAD box helicase family. 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