Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P38132

- MCM7_YEAST

UniProt

P38132 - MCM7_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. 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
Complete GO annotation...

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.
ReactomeiREACT_241537. Switching of origins to a post-replicative state.
REACT_245084. Removal of licensing factors from origins.
REACT_255883. Unwinding of DNA.

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
Complete GO annotation...

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. 40 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.
InParanoidiP38132.
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

        10         20         30         40         50
MSAALPSIQL PVDYNNLFNE ITDFLVTFKQ DTLSSDATRN ENEDENLDAE
60 70 80 90 100
NIEQHLLEKG PKYMAMLQKV ANRELNSVII DLDDILQYQN EKFLQGTQAD
110 120 130 140 150
DLVSAIQQNA NHFTELFCRA IDNNMPLPTK EIDYKDDVLD VILNQRRLRN
160 170 180 190 200
ERMLSDRTNE IRSENLMDTT MDPPSSMNDA LREVVEDETE LFPPNLTRRY
210 220 230 240 250
FLYFKPLSQN CARRYRKKAI SSKPLSVRQI KGDFLGQLIT VRGIITRVSD
260 270 280 290 300
VKPAVEVIAY TCDQCGYEVF QEVNSRTFTP LSECTSEECS QNQTKGQLFM
310 320 330 340 350
STRASKFSAF QECKIQELSQ QVPVGHIPRS LNIHVNGTLV RSLSPGDIVD
360 370 380 390 400
VTGIFLPAPY TGFKALKAGL LTETYLEAQF VRQHKKKFAS FSLTSDVEER
410 420 430 440 450
VMELITSGDV YNRLAKSIAP EIYGNLDVKK ALLLLLVGGV DKRVGDGMKI
460 470 480 490 500
RGDINVCLMG DPGVAKSQLL KAICKISPRG VYTTGKGSSG VGLTAAVMKD
510 520 530 540 550
PVTDEMILEG GALVLADNGI CCIDEFDKMD ESDRTAIHEV MEQQTISISK
560 570 580 590 600
AGINTTLNAR TSILAAANPL YGRYNPRLSP LDNINLPAAL LSRFDILFLM
610 620 630 640 650
LDIPSRDDDE KLAEHVTYVH MHNKQPDLDF TPVEPSKMRE YIAYAKTKRP
660 670 680 690 700
VMSEAVNDYV VQAYIRLRQD SKREMDSKFS FGQATPRTLL GIIRLSQALA
710 720 730 740 750
KLRLADMVDI DDVEEALRLV RVSKESLYQE TNKSKEDESP TTKIFTIIKK
760 770 780 790 800
MLQETGKNTL SYENIVKTVR LRGFTMLQLS NCIQEYSYLN VWHLINEGNT
810 820 830 840
LKFVDDGTMD TDQEDSLVST PKLAPQTTAS ANVSAQDSDI DLQDA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 40 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.
InParanoidi P38132.
KOi K02210.
OMAi DINICLM.
OrthoDBi EOG7Z69MX.

Enzyme and pathway databases

BioCyci YEAST:G3O-29143-MONOMER.
Reactomei REACT_241537. Switching of origins to a post-replicative state.
REACT_245084. Removal of licensing factors from origins.
REACT_255883. Unwinding of DNA.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 144 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