3'-5' DNA helicase and substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks (By similarity). Involved in genome maintenance by acting as an anti-recombinogenic helicase and preventing extensive strand exchange during homologous recombination: promotes RAD51 filament dissolution from stalled forks, thereby inhibiting homologous recombination and preventing excessive recombination (PubMed:24108124). Also promotes cell death and DNA double-strand breakage in response to replication stress: together with MUS81, promotes the endonucleolytic DNA cleavage following prolonged replication stress via its helicase activity, possibly to eliminate cells with excessive replication stress. Plays a major role in remodeling of stalled DNA forks by catalyzing fork regression, in which the fork reverses and the two nascent DNA strands anneal. In addition to the helicase activity, also acts as the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex, a complex that mediates ubiquitination of RAD51, leading to regulate RAD51 subcellular location (By similarity). ATP + H2O = ADP + H(+) + phosphate Protein modification; protein ubiquitination. Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBH1) composed of CUL1, SKP1, RBX1 and FBH1 (By similarity). Interacts with RPA2 (By similarity). Interacts with RAD51 (PubMed:24108124). Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA (By similarity). Accumulates at sites of DNA damage or replication stress. PCNA is required for localization to DNA damage sites. Localizes to the nucleoplasm in absence of DNA damage. The PIP-box mediates the interaction with PCNA. Ubiquitinated. Ubiquitination by the DCX(DTL) complex, also named CRL4(CDT2), leading to its degradation: ubiquitination takes place after its localization to DNA damage sites, possibly to facilitate the translesion synthesis (TLS) pathway. Belongs to the helicase family. UvrD subfamily.