Taxonomic distribution of proteins containing MCM domains

The MCM domain within your query sequence starts at position 290 and ends at position 803, and its E-value is < 1e-12.

MCM proteins: evolution, properties, and role in DNA replication.

Kearsey SE, Labib K
Biochim Biophys Acta. 1998; 1398: 113-36

The AAA team: related ATPases with diverse functions.

Patel S, Latterich M
Trends Cell Biol. 1998; 8: 65-71

A new family of related ATPases has emerged, characterized by a highly conserved AAA motif. This motif forms a 230-amino-acid domain that contains Walker homology sequences and imparts ATPase activity. Homology between AAA-family members is confined mostly to the AAA domain, although additional homology outside the AAA motif is present among closely related proteins. AAA proteins act in a variety of cellular functions, including cell-cycle regulation, protein degradation, organelle biogenesis and vesicle-mediated protein transport. The AAA domain is required for protein function, but its exact role and the specific activity that it confers on AAA proteins is still unclear. This review describes current understanding of the AAA protein family.

The role of MCM/P1 proteins in the licensing of DNA replication.

Chong JP, Thommes P, Blow JJ
Trends Biochem Sci. 1996; 21: 102-6

The DNA replication licensing system ensures that eukaryotic chromosomes replicate precisely once per cell cycle. A central component of the licensing system, RLF-M, has recently been shown to consist of a complex of Mcm/P1 proteins. This result allows us to integrate data about the MCM/P1 family obtained in different eukaryotes, ranging from yeast to man, into a general picture of the way that chromosome replication is controlled.

A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication.

Koonin EV
Nucleic Acids Res. 1993; 21: 2541-7

A new superfamily of (putative) DNA-dependent ATPases is described that includes the ATPase domains of prokaryotic NtrC-related transcription regulators, MCM proteins involved in the initiation of eukaryotic DNA replication, and a group of uncharacterized bacterial and chloroplast proteins. MCM proteins are shown to contain a modified form of the ATP-binding motif and are predicted to mediate ATP-dependent opening of double-stranded DNA in the replication origins. In a second line of investigation, it is demonstrated that the products of unidentified open reading frames from Marchantia mitochondria and from yeast, and a domain of a baculovirus protein involved in viral DNA replication are related to the superfamily III of DNA and RNA helicases that previously has been known to include only proteins of small viruses. Comparison of the multiple alignments showed that the proteins of the NtrC superfamily and the helicases of superfamily III share three related sequence motifs tightly packed in the ATPase domain that consists of 100-150 amino acid residues. A similar array of conserved motifs is found in the family of DnaA-related ATPases. It is hypothesized that the three large groups of nucleic acid-dependent ATPases have similar structure of the core ATPase domain and have evolved from a common ancestor.