SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed=25618846)
Hetero octamer : IID00058Complex,IID00239Complex
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed=25618846)
Hetero tetramer : IID00058Complex,IID00088Complex
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed=25618846)
Hetero tetramer : IID00058Complex,IID00062Complex,IID00182Complex
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed=25618846)
Hetero hexamer : IID00058Complex,IID00239Complex
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed=25618846)
Hetero tetramer : IID00058Complex,IID00062Complex
SeqProS verified 68-125 The residues 107-122 form a helical conformation in the free state (PubMed=25618846)
Hetero tetramer : IID00058Complex,IID00239Complex
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division. Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis.