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P38132 (MCM7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA replication licensing factor MCM7

EC=3.6.4.12
Alternative name(s):
Cell division control protein 47
Minichromosome maintenance protein 7
Gene names
Name:MCM7
Synonyms:CDC47
Ordered Locus Names:YBR202W
ORF Names:YBR1441
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length845 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Ref.8 Ref.9

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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 CSM1 and MCM10. Ref.8 Ref.9 Ref.10 Ref.13

Subcellular location

Cytoplasm. Nucleus Ref.11.

Miscellaneous

Present with 166 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.

Sequence similarities

Belongs to the MCM family.

Contains 1 MCM domain.

Ontologies

Keywords
   Biological processCell cycle
DNA replication
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 15723534. Source: GOC

DNA replication initiation

Inferred from mutant phenotype PubMed 10783164PubMed 2044962. Source: SGD

DNA strand elongation involved in DNA replication

Inferred from mutant phenotype PubMed 10783164PubMed 10834843. Source: SGD

DNA unwinding involved in DNA replication

Inferred from direct assay PubMed 13679365PubMed 15723534. Source: SGD

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype PubMed 19064704. Source: SGD

chromatin silencing at telomere

Inferred from mutant phenotype PubMed 19064704. Source: SGD

double-strand break repair via break-induced replication

Inferred from mutant phenotype PubMed 20516198. Source: SGD

nuclear cell cycle DNA replication

Inferred from mutant phenotype PubMed 10834843PubMed 2044962. Source: SGD

pre-replicative complex assembly involved in nuclear cell cycle DNA replication

Inferred from direct assay PubMed 16824194. Source: SGD

   Cellular_componentDNA replication preinitiation complex

Inferred from direct assay PubMed 9554851. Source: SGD

MCM complex

Inferred from direct assay PubMed 12480933. Source: SGD

MCM core complex

Inferred from direct assay PubMed 13679365. Source: SGD

cytoplasm

Inferred from direct assay PubMed 10704410Ref.1. Source: SGD

nuclear pre-replicative complex

Inferred from direct assay PubMed 16824194PubMed 9335335. Source: SGD

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10704410Ref.1. Source: SGD

replication fork protection complex

Inferred from direct assay PubMed 16531994. Source: SGD

   Molecular_functionATP binding

Inferred from direct assay PubMed 12480933. Source: SGD

DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA replication origin binding

Inferred from direct assay PubMed 11756674PubMed 16824194PubMed 9288745. Source: SGD

chromatin binding

Inferred from direct assay PubMed 9159120PubMed 9288745. Source: SGD

protein binding

Inferred from physical interaction PubMed 11805826PubMed 12480933Ref.13PubMed 16429126Ref.8PubMed 22433841. Source: IntAct

single-stranded DNA-dependent ATPase activity

Inferred from direct assay PubMed 15723534. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 845845DNA replication licensing factor MCM7
PRO_0000194124

Regions

Domain410 – 617208MCM
Nucleotide binding460 – 4678ATP Potential
Motif592 – 5954Arginine finger

Amino acid modifications

Modified residue8111Phosphothreonine Ref.5 Ref.7
Modified residue8191Phosphoserine Ref.7
Modified residue8381Phosphoserine Ref.14

Experimental info

Mutagenesis4661K → A: Loss of MCM2-7 complex helicase activity. Ref.6
Sequence conflict5521G → V in CAA79689. Ref.2
Sequence conflict5521G → V in CAA85166. Ref.3
Sequence conflict556 – 5583TLN → NPG in CAA79689. Ref.2
Sequence conflict556 – 5583TLN → NPG in CAA85166. Ref.3
Sequence conflict5741Y → I in CAA79689. Ref.2
Sequence conflict5741Y → I in CAA85166. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P38132 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: ADA66C719D96DB4A

FASTA84594,943
        10         20         30         40         50         60 
MSAALPSIQL PVDYNNLFNE ITDFLVTFKQ DTLSSDATRN ENEDENLDAE NIEQHLLEKG 

        70         80         90        100        110        120 
PKYMAMLQKV ANRELNSVII DLDDILQYQN EKFLQGTQAD DLVSAIQQNA NHFTELFCRA 

       130        140        150        160        170        180 
IDNNMPLPTK EIDYKDDVLD VILNQRRLRN ERMLSDRTNE IRSENLMDTT MDPPSSMNDA 

       190        200        210        220        230        240 
LREVVEDETE LFPPNLTRRY FLYFKPLSQN CARRYRKKAI SSKPLSVRQI KGDFLGQLIT 

       250        260        270        280        290        300 
VRGIITRVSD VKPAVEVIAY TCDQCGYEVF QEVNSRTFTP LSECTSEECS QNQTKGQLFM 

       310        320        330        340        350        360 
STRASKFSAF QECKIQELSQ QVPVGHIPRS LNIHVNGTLV RSLSPGDIVD VTGIFLPAPY 

       370        380        390        400        410        420 
TGFKALKAGL LTETYLEAQF VRQHKKKFAS FSLTSDVEER VMELITSGDV YNRLAKSIAP 

       430        440        450        460        470        480 
EIYGNLDVKK ALLLLLVGGV DKRVGDGMKI RGDINVCLMG DPGVAKSQLL KAICKISPRG 

       490        500        510        520        530        540 
VYTTGKGSSG VGLTAAVMKD PVTDEMILEG GALVLADNGI CCIDEFDKMD ESDRTAIHEV 

       550        560        570        580        590        600 
MEQQTISISK AGINTTLNAR TSILAAANPL YGRYNPRLSP LDNINLPAAL LSRFDILFLM 

       610        620        630        640        650        660 
LDIPSRDDDE KLAEHVTYVH MHNKQPDLDF TPVEPSKMRE YIAYAKTKRP VMSEAVNDYV 

       670        680        690        700        710        720 
VQAYIRLRQD SKREMDSKFS FGQATPRTLL GIIRLSQALA KLRLADMVDI DDVEEALRLV 

       730        740        750        760        770        780 
RVSKESLYQE TNKSKEDESP TTKIFTIIKK MLQETGKNTL SYENIVKTVR LRGFTMLQLS 

       790        800        810        820        830        840 
NCIQEYSYLN VWHLINEGNT LKFVDDGTMD TDQEDSLVST PKLAPQTTAS ANVSAQDSDI 


DLQDA 

« Hide

References

« Hide 'large scale' references
[1]"Cell cycle-regulated nuclear import and export of Cdc47, a protein essential for initiation of DNA replication in budding yeast."
Dalton S., Whitbread L.
Proc. Natl. Acad. Sci. U.S.A. 92:2514-2518(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A 12.8 kb segment, on the right arm of chromosome II from Saccharomyces cerevisiae including part of the DUR1,2 gene, contains five putative new genes."
Bussereau F., Mallet L., Gaillon L., Jacquet M.
Yeast 9:797-806(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 552; 556-558 AND 574.
Strain: ATCC 204508 / S288c.
[5]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-811, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[6]"The Mcm2-7 complex has in vitro helicase activity."
Bochman M.L., Schwacha A.
Mol. Cell 31:287-293(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7 COMPLEX, MUTAGENESIS OF LYS-466.
[7]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-811 AND SER-819, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing."
Remus D., Beuron F., Tolun G., Griffith J.D., Morris E.P., Diffley J.F.
Cell 139:719-730(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
[9]"A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication."
Evrin C., Clarke P., Zech J., Lurz R., Sun J., Uhle S., Li H., Stillman B., Speck C.
Proc. Natl. Acad. Sci. U.S.A. 106:20240-20245(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
[10]"A lesion in the DNA replication initiation factor Mcm10 induces pausing of elongation forks through chromosomal replication origins in Saccharomyces cerevisiae."
Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K.
Mol. Cell. Biol. 17:3261-3271(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCM10.
[11]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]"Saccharomyces cerevisiae CSM1 gene encoding a protein influencing chromosome segregation in meiosis I interacts with elements of the DNA replication complex."
Wysocka M., Rytka J., Kurlandzka A.
Exp. Cell Res. 294:592-602(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSM1.
[14]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-838, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14730 Genomic DNA. Translation: AAA86309.1.
Z21487 Genomic DNA. Translation: CAA79689.1.
Z36071 Genomic DNA. Translation: CAA85166.1.
BK006936 Genomic DNA. Translation: DAA07320.2.
PIRS34027.
RefSeqNP_009761.4. NM_001178550.4.

3D structure databases

ProteinModelPortalP38132.
SMRP38132. Positions 131-355, 409-729.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32899. 39 interactions.
DIPDIP-2408N.
IntActP38132. 11 interactions.
MINTMINT-637194.
STRING4932.YBR202W.

Proteomic databases

MaxQBP38132.
PaxDbP38132.
PeptideAtlasP38132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR202W; YBR202W; YBR202W.
GeneID852501.
KEGGsce:YBR202W.

Organism-specific databases

CYGDYBR202w.
SGDS000000406. MCM7.

Phylogenomic databases

eggNOGCOG1241.
GeneTreeENSGT00670000098113.
KOK02210.
OMADINICLM.
OrthoDBEOG7Z69MX.

Enzyme and pathway databases

BioCycYEAST:G3O-29143-MONOMER.
ReactomeREACT_190740. Cell Cycle.

Gene expression databases

GenevestigatorP38132.

Family and domain databases

Gene3D2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR008050. MCM7.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11630:SF26. PTHR11630:SF26. 1 hit.
PfamPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSPR01657. MCMFAMILY.
PR01663. MCMPROTEIN7.
SMARTSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971507.
PROP38132.

Entry information

Entry nameMCM7_YEAST
AccessionPrimary (citable) accession number: P38132
Secondary accession number(s): D6VQK0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families