DNA-dependent ATPase component of the Fanconi anemia (FA) core complex (PubMed:16116422). Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:16116422, PubMed:19423727, PubMed:20347428, PubMed:20347429, PubMed:29231814). In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates (PubMed:20347428, PubMed:20347429). Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX (PubMed:20347429). In complex with FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates (PubMed:17289582). In vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA (PubMed:16116434). ATP + H2O = ADP + H(+) + phosphate Component of the Fanconi anemia (FA) core complex, which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FAAP24 and FAAP100 (PubMed:16116422, PubMed:16116434, PubMed:17289582). The FA core complex associates with Bloom syndrome (BLM) complex, which consists of at least BLM, DNA topoisomerase 3-alpha/TOP3A, RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32. This supercomplex between FA and BLM complexes has been called BRAFT (PubMed:20347428). Forms a discrete complex with CENPS and CENPX, called FANCM-MHF; this interaction stimulates DNA binding and replication fork remodeling by FANCM and stabilizes the binding partners (PubMed:20347428, PubMed:20347429). Forms a heterodimer with FAAP24; this interaction increases FANCM single-stranded DNA-binding activity (PubMed:17289582, PubMed:20347428). Expressed in germ cells of fetal and adult ovaries. In fetal ovaries, it is present in oogonia but expression is stronger in pachytene stage oocytes. Expressed in oocytes arrested at the diplotene stage of prophase I during the last trimester of pregnancy and in adults (PubMed:29231814). Expressed in the testis (PubMed:30075111). Expressed throughout ovarian development (5-32 weeks post-fertilization (wpf)). Expression tends to be higher at 14 and 17 wpf. Phosphorylated; hyperphosphorylated in response to genotoxic stress. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily. Intron retention.