P53091 · MCM6_YEAST
- ProteinDNA replication licensing factor MCM6
- GeneMCM6
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1017 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a 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. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for the entry in S phase and for cell division.
Miscellaneous
Present with 13400 molecules/cell in log phase SD medium.
Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA replication licensing factor MCM6
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP53091
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 581 | Loss of MCM2-7 complex helicase activity. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 9 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000194117 | 1-1017 | DNA replication licensing factor MCM6 | |||
Sequence: MSSPFPADTPSSNRPSNSSPPPSSIGAGFGSSSGLDSQIGSRLHFPSSSQPHVSNSQTGPFVNDSTQFSSQRLQTDGSATNDMEGNEPARSFKSRALNHVKKVDDVTGEKVREAFEQFLEDFSVQSTDTGEVEKVYRAQIEFMKIYDLNTIYIDYQHLSMRENGALAMAISEQYYRFLPFLQKGLRRVVRKYAPELLNTSDSLKRSEGDEGQADEDEQQDDDMNGSSLPRDSGSSAAPGNGTSAMATRSITTSTSPEQTERVFQISFFNLPTVHRIRDIRSEKIGSLLSISGTVTRTSEVRPELYKASFTCDMCRAIVDNVEQSFKYTEPTFCPNPSCENRAFWTLNVTRSRFLDWQKVRIQENANEIPTGSMPRTLDVILRGDSVERAKPGDRCKFTGVEIVVPDVTQLGLPGVKPSSTLDTRGISKTTEGLNSGVTGLRSLGVRDLTYKISFLACHVISIGSNIGASSPDANSNNRETELQMAANLQANNVYQDNERDQEVFLNSLSSDEINELKEMVKDEHIYDKLVRSIAPAVFGHEAVKKGILLQMLGGVHKSTVEGIKLRGDINICVVGDPSTSKSQFLKYVVGFAPRSVYTSGKASSAAGLTAAVVRDEEGGDYTIEAGALMLADNGICCIDEFDKMDISDQVAIHEAMEQQTISIAKAGIHATLNARTSILAAANPVGGRYNRKLSLRGNLNMTAPIMSRFDLFFVILDDCNEKIDTELASHIVDLHMKRDEAIEPPFSAEQLRRYIKYARTFKPILTKEARSYLVEKYKELRKDDAQGFSRSSYRITVRQLESMIRLSEAIARANCVDEITPSFIAEAYDLLRQSIIRVDVDDVEMDEEFDNIESQSHAASGNNDDNDDGTGSGVITSEPPADIEEGQSEATARPGTSEKKKTTVTYDKYVSMMNMIVRKIAEVDREGAEELTAVDIVDWYLLQKENDLGSLAEYWEERRLAFKVIKRLVKDRILMEIHGTRHNLRDLENEENENNKTVYVIHPNCEVLDQLEPQDSS | ||||||
Modified residue | 78 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 249 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 372 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 766 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer. Interacts with MCM10.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P53091 | MCM10 P32354 | 6 | EBI-10556, EBI-5965 | |
BINARY | P53091 | MCM4 P30665 | 8 | EBI-10556, EBI-4326 | |
BINARY | P53091 | SMT3 Q12306 | 2 | EBI-10556, EBI-17490 | |
BINARY | P53091 | TAH11 P47112 | 4 | EBI-10556, EBI-25503 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-87 | Polar residues | ||||
Sequence: MSSPFPADTPSSNRPSNSSPPPSSIGAGFGSSSGLDSQIGSRLHFPSSSQPHVSNSQTGPFVNDSTQFSSQRLQTDGSATNDMEGNE | ||||||
Region | 1-94 | Disordered | ||||
Sequence: MSSPFPADTPSSNRPSNSSPPPSSIGAGFGSSSGLDSQIGSRLHFPSSSQPHVSNSQTGPFVNDSTQFSSQRLQTDGSATNDMEGNEPARSFKS | ||||||
Region | 200-257 | Disordered | ||||
Sequence: SDSLKRSEGDEGQADEDEQQDDDMNGSSLPRDSGSSAAPGNGTSAMATRSITTSTSPE | ||||||
Compositional bias | 225-257 | Polar residues | ||||
Sequence: GSSLPRDSGSSAAPGNGTSAMATRSITTSTSPE | ||||||
Domain | 525-732 | MCM | ||||
Sequence: IYDKLVRSIAPAVFGHEAVKKGILLQMLGGVHKSTVEGIKLRGDINICVVGDPSTSKSQFLKYVVGFAPRSVYTSGKASSAAGLTAAVVRDEEGGDYTIEAGALMLADNGICCIDEFDKMDISDQVAIHEAMEQQTISIAKAGIHATLNARTSILAAANPVGGRYNRKLSLRGNLNMTAPIMSRFDLFFVILDDCNEKIDTELASHIV | ||||||
Motif | 707-710 | Arginine finger | ||||
Sequence: SRFD | ||||||
Region | 852-901 | Disordered | ||||
Sequence: IESQSHAASGNNDDNDDGTGSGVITSEPPADIEEGQSEATARPGTSEKKK | ||||||
Compositional bias | 854-873 | Polar residues | ||||
Sequence: SQSHAASGNNDDNDDGTGSG |
Sequence similarities
Belongs to the MCM family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,017
- Mass (Da)112,978
- Last updated2010-10-05 v2
- Checksum03AB793134E64A50
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-87 | Polar residues | ||||
Sequence: MSSPFPADTPSSNRPSNSSPPPSSIGAGFGSSSGLDSQIGSRLHFPSSSQPHVSNSQTGPFVNDSTQFSSQRLQTDGSATNDMEGNE | ||||||
Sequence conflict | 179 | in Ref. 2; CAA96913 | ||||
Sequence: P → A | ||||||
Compositional bias | 225-257 | Polar residues | ||||
Sequence: GSSLPRDSGSSAAPGNGTSAMATRSITTSTSPE | ||||||
Compositional bias | 854-873 | Polar residues | ||||
Sequence: SQSHAASGNNDDNDDGTGSG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY258324 EMBL· GenBank· DDBJ | AAO89010.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z72723 EMBL· GenBank· DDBJ | CAA96913.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y13624 EMBL· GenBank· DDBJ | CAA73947.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006941 EMBL· GenBank· DDBJ | DAA07914.1 EMBL· GenBank· DDBJ | Genomic DNA |