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P38132

- MCM7_YEAST

UniProt

P38132 - MCM7_YEAST

Protein

DNA replication licensing factor MCM7

Gene

MCM7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi460 – 4678ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: SGD
    2. chromatin binding Source: SGD
    3. DNA helicase activity Source: InterPro
    4. DNA replication origin binding Source: SGD
    5. protein binding Source: IntAct
    6. single-stranded DNA-dependent ATPase activity Source: SGD

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. chromatin silencing at silent mating-type cassette Source: SGD
    3. chromatin silencing at telomere Source: SGD
    4. DNA replication initiation Source: SGD
    5. DNA strand elongation involved in DNA replication Source: SGD
    6. DNA unwinding involved in DNA replication Source: SGD
    7. double-strand break repair via break-induced replication Source: SGD
    8. nuclear cell cycle DNA replication Source: SGD
    9. pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: SGD

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, DNA replication

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29143-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA replication licensing factor MCM7 (EC:3.6.4.12)
    Alternative name(s):
    Cell division control protein 47
    Minichromosome maintenance protein 7
    Gene namesi
    Name:MCM7
    Synonyms:CDC47
    Ordered Locus Names:YBR202W
    ORF Names:YBR1441
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR202w.
    SGDiS000000406. MCM7.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. DNA replication preinitiation complex Source: SGD
    3. MCM complex Source: SGD
    4. MCM core complex Source: SGD
    5. nuclear pre-replicative complex Source: SGD
    6. nucleoplasm Source: Reactome
    7. nucleus Source: SGD
    8. replication fork protection complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi466 – 4661K → A: Loss of MCM2-7 complex helicase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 845845DNA replication licensing factor MCM7PRO_0000194124Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei811 – 8111Phosphothreonine2 Publications
    Modified residuei819 – 8191Phosphoserine1 Publication
    Modified residuei838 – 8381Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38132.
    PaxDbiP38132.
    PeptideAtlasiP38132.

    Expressioni

    Gene expression databases

    GenevestigatoriP38132.

    Interactioni

    Subunit structurei

    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 MCM10.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSM1P256513EBI-4300,EBI-22001
    ERG26P531992EBI-4300,EBI-6514
    MCM4P306653EBI-4300,EBI-4326

    Protein-protein interaction databases

    BioGridi32899. 39 interactions.
    DIPiDIP-2408N.
    IntActiP38132. 11 interactions.
    MINTiMINT-637194.
    STRINGi4932.YBR202W.

    Structurei

    3D structure databases

    ProteinModelPortaliP38132.
    SMRiP38132. Positions 131-355, 409-729.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini410 – 617208MCMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi592 – 5954Arginine finger

    Sequence similaritiesi

    Belongs to the MCM family.Curated
    Contains 1 MCM domain.Curated

    Phylogenomic databases

    eggNOGiCOG1241.
    GeneTreeiENSGT00670000098113.
    KOiK02210.
    OMAiDINICLM.
    OrthoDBiEOG7Z69MX.

    Family and domain databases

    Gene3Di2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR003593. 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]
    PANTHERiPTHR11630:SF26. PTHR11630:SF26. 1 hit.
    PfamiPF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01657. MCMFAMILY.
    PR01663. MCMPROTEIN7.
    SMARTiSM00382. AAA. 1 hit.
    SM00350. MCM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38132-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAALPSIQL PVDYNNLFNE ITDFLVTFKQ DTLSSDATRN ENEDENLDAE    50
    NIEQHLLEKG PKYMAMLQKV ANRELNSVII DLDDILQYQN EKFLQGTQAD 100
    DLVSAIQQNA NHFTELFCRA IDNNMPLPTK EIDYKDDVLD VILNQRRLRN 150
    ERMLSDRTNE IRSENLMDTT MDPPSSMNDA LREVVEDETE LFPPNLTRRY 200
    FLYFKPLSQN CARRYRKKAI SSKPLSVRQI KGDFLGQLIT VRGIITRVSD 250
    VKPAVEVIAY TCDQCGYEVF QEVNSRTFTP LSECTSEECS QNQTKGQLFM 300
    STRASKFSAF QECKIQELSQ QVPVGHIPRS LNIHVNGTLV RSLSPGDIVD 350
    VTGIFLPAPY TGFKALKAGL LTETYLEAQF VRQHKKKFAS FSLTSDVEER 400
    VMELITSGDV YNRLAKSIAP EIYGNLDVKK ALLLLLVGGV DKRVGDGMKI 450
    RGDINVCLMG DPGVAKSQLL KAICKISPRG VYTTGKGSSG VGLTAAVMKD 500
    PVTDEMILEG GALVLADNGI CCIDEFDKMD ESDRTAIHEV MEQQTISISK 550
    AGINTTLNAR TSILAAANPL YGRYNPRLSP LDNINLPAAL LSRFDILFLM 600
    LDIPSRDDDE KLAEHVTYVH MHNKQPDLDF TPVEPSKMRE YIAYAKTKRP 650
    VMSEAVNDYV VQAYIRLRQD SKREMDSKFS FGQATPRTLL GIIRLSQALA 700
    KLRLADMVDI DDVEEALRLV RVSKESLYQE TNKSKEDESP TTKIFTIIKK 750
    MLQETGKNTL SYENIVKTVR LRGFTMLQLS NCIQEYSYLN VWHLINEGNT 800
    LKFVDDGTMD TDQEDSLVST PKLAPQTTAS ANVSAQDSDI DLQDA 845
    Length:845
    Mass (Da):94,943
    Last modified:July 27, 2011 - v4
    Checksum:iADA66C719D96DB4A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti552 – 5521G → V in CAA79689. (PubMed:8368014)Curated
    Sequence conflicti552 – 5521G → V in CAA85166. (PubMed:7813418)Curated
    Sequence conflicti556 – 5583TLN → NPG in CAA79689. (PubMed:8368014)Curated
    Sequence conflicti556 – 5583TLN → NPG in CAA85166. (PubMed:7813418)Curated
    Sequence conflicti574 – 5741Y → I in CAA79689. (PubMed:8368014)Curated
    Sequence conflicti574 – 5741Y → I in CAA85166. (PubMed:7813418)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14730 Genomic DNA. Translation: AAA86309.1.
    Z21487 Genomic DNA. Translation: CAA79689.1.
    Z36071 Genomic DNA. Translation: CAA85166.1.
    BK006936 Genomic DNA. Translation: DAA07320.2.
    PIRiS34027.
    RefSeqiNP_009761.4. NM_001178550.4.

    Genome annotation databases

    EnsemblFungiiYBR202W; YBR202W; YBR202W.
    GeneIDi852501.
    KEGGisce:YBR202W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14730 Genomic DNA. Translation: AAA86309.1 .
    Z21487 Genomic DNA. Translation: CAA79689.1 .
    Z36071 Genomic DNA. Translation: CAA85166.1 .
    BK006936 Genomic DNA. Translation: DAA07320.2 .
    PIRi S34027.
    RefSeqi NP_009761.4. NM_001178550.4.

    3D structure databases

    ProteinModelPortali P38132.
    SMRi P38132. Positions 131-355, 409-729.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32899. 39 interactions.
    DIPi DIP-2408N.
    IntActi P38132. 11 interactions.
    MINTi MINT-637194.
    STRINGi 4932.YBR202W.

    Proteomic databases

    MaxQBi P38132.
    PaxDbi P38132.
    PeptideAtlasi P38132.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR202W ; YBR202W ; YBR202W .
    GeneIDi 852501.
    KEGGi sce:YBR202W.

    Organism-specific databases

    CYGDi YBR202w.
    SGDi S000000406. MCM7.

    Phylogenomic databases

    eggNOGi COG1241.
    GeneTreei ENSGT00670000098113.
    KOi K02210.
    OMAi DINICLM.
    OrthoDBi EOG7Z69MX.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29143-MONOMER.

    Miscellaneous databases

    NextBioi 971507.
    PROi P38132.

    Gene expression databases

    Genevestigatori P38132.

    Family and domain databases

    Gene3Di 2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR003593. 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 ]
    PANTHERi PTHR11630:SF26. PTHR11630:SF26. 1 hit.
    Pfami PF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01657. MCMFAMILY.
    PR01663. MCMPROTEIN7.
    SMARTi SM00382. AAA. 1 hit.
    SM00350. MCM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. 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].

    Entry informationi

    Entry nameiMCM7_YEAST
    AccessioniPrimary (citable) accession number: P38132
    Secondary accession number(s): D6VQK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 142 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 166 molecules/cell in log phase SD medium.1 Publication
    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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3