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May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP-dependent breakage, passage and rejoining of double-stranded DNA.","ecNumber":"5.6.2.2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19222228"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19697956"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19222228"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19697956"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22323612"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22841979"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19222228"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19697956"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22323612"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22841979"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19222228"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19697956"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22323612"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22841979"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19222228"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19697956"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22323612"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22841979"}],"value":"Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+)."}]}},{"texts":[{"value":"Specifically inhibited by the intercalating agent amsacrine"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P41516"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q01320"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12711669"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15126503"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16100112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17567603"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20457750"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22013166"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22841979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23213405"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23652018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26030138"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27754753"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36271492"}],"value":"Homodimer. 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Interacts with POL1RA/RPA1 (via dock II) and UBTF in the context of Pol I complex; may assist Pol I transcription initiation by releasing supercoils occurring during DNA unwinding. Interacts with TPRN; TPRN interacts with a number of DNA damage response proteins, is recruited to sites of DNA damage and may play a role in DNA damage repair (PubMed:23213405). 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Also found in high-grade lymphomas, squamous cell lung tumors and seminomas (PubMed:9155056)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0AES6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25202966"}],"value":"The N-terminus has several structural domains; the ATPase domain (about residues 1-265), the transducer domain (about 266-428) and the toprim domain (455-572) (PubMed:25202966). Comparing different structures shows ATP hydrolysis induces domain shifts in the N-terminus that are probably part of the mechanism of DNA cleavage and rejoining (PubMed:25202966)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10942766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18062778"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19043076"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.11"}],"value":"Phosphorylation has no effect on catalytic activity. 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