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Acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination (PubMed:14983014, PubMed:16153896). Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1 (PubMed:14983014, PubMed:16153896). Involved in the repair of abasic sites at replication forks by promoting the degradation of DNA-protein cross-links: acts by catalyzing unfolding of HMCES DNA-protein cross-link via its helicase activity, exposing the underlying DNA and enabling cleavage of the DNA-protein adduct by the SPRTN metalloprotease (PubMed:16116421, PubMed:36608669). Can unwind RNA:DNA substrates (PubMed:14983014). Unwinds G-quadruplex DNA; unwinding requires a 5'-single stranded tail (PubMed:18426915, PubMed:20639400)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14983014"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20639400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36608669"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14983014"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20639400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36608669"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16973432"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20639400"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20639400"}],"value":"Binds 1 [4Fe-4S] cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17596542"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18426915"}],"value":"Helicase activity on forked substrates is stimulated by replication protein A complex heterotrimer (RPA1, RPA2, RPA3) (PubMed:17596542). Helicase activity on G-quadruplex DNA is stimulated 3-fold by RPA, and inhibited by MSH2/MSH6 (PubMed:18426915). Unwinding of G-quadruplex DNA is inhibited by ATP-gamma-S and telomestatin (TMS); TMA does not inhibit unwinding of forked-duplex DNA (PubMed:18426915). Helicase activity on dsDNA and G-quadruplex DNA is inhibited by porphyrin derivatives meso-tetra (N-methyl-4-pyridyl) porphine tetra tosylate (T4) and N-methyl mesoporphyrin IX (NMM) (PubMed:18426915)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15125843"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17596542"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23585563"}],"value":"Interacts with the replication protein A complex (RPA) via the RPA1 subunit; following DNA damage they colocalize in foci in the nucleus (PubMed:17596542). Binds directly to the BRCT domains of BRCA1 (PubMed:15125843). Interacts with the CIA complex components CIAO1, CIAO2B and MMS19 (PubMed:23585563)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9BX63","intActId":"EBI-3509650"},"interactantTwo":{"uniProtKBAccession":"P54132","geneName":"BLM","intActId":"EBI-621372"},"numberOfExperiments":16,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9BX63","intActId":"EBI-3509650"},"interactantTwo":{"uniProtKBAccession":"P38398","geneName":"BRCA1","intActId":"EBI-349905"},"numberOfExperiments":29,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9BX63","intActId":"EBI-3509650"},"interactantTwo":{"uniProtKBAccession":"Q9BPX1","geneName":"HSD17B14","intActId":"EBI-742664"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9BX63","intActId":"EBI-3509650"},"interactantTwo":{"uniProtKBAccession":"P40692","geneName":"MLH1","intActId":"EBI-744248"},"numberOfExperiments":21,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9BX63","intActId":"EBI-3509650"},"interactantTwo":{"uniProtKBAccession":"Q96T76","geneName":"MMS19","intActId":"EBI-1044169"},"numberOfExperiments":4,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11301010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17596542"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23585563"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23585563"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q9BX63-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q9BX63-2"],"sequenceIds":["VSP_012540","VSP_012541"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11301010"}],"value":"Ubiquitously expressed, with highest levels in testis"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20639400"}],"value":"4Fe-4S iron-sulfur-binding is required for helicase activity"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14576433"}],"value":"Phosphorylated. 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