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Protein

DNA replication licensing factor MCM4

Gene

MCM4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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. Required for S phase execution.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi568 – 5758ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA helicase activity Source: InterPro
  • DNA replication origin binding Source: SGD
  • single-stranded DNA binding Source: SGD

GO - Biological processi

  • DNA replication initiation Source: SGD
  • DNA strand elongation involved in DNA replication Source: SGD
  • DNA unwinding involved in DNA replication Source: SGD
  • double-strand break repair via break-induced replication Source: SGD
  • nuclear DNA replication Source: SGD
  • 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-34179-MONOMER.
ReactomeiR-SCE-176974. Unwinding of DNA.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69052. Switching of origins to a post-replicative state.
R-SCE-69300. Removal of licensing factors from origins.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM4 (EC:3.6.4.12)
Alternative name(s):
Cell division control protein 54
Gene namesi
Name:MCM4
Synonyms:CDC54, HCD21
Ordered Locus Names:YPR019W
ORF Names:YP9531.13
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR019W.
SGDiS000006223. MCM4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • DNA replication preinitiation complex Source: SGD
  • MCM complex Source: SGD
  • MCM core complex Source: SGD
  • nuclear pre-replicative complex Source: SGD
  • nuclear replication fork Source: SGD
  • nucleoplasm Source: Reactome
  • nucleus Source: SGD
  • replication fork protection complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi574 – 5741K → A: Loss of MCM2-7 complex helicase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 933933DNA replication licensing factor MCM4PRO_0000194105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521PhosphoserineCombined sources
Modified residuei56 – 561PhosphoserineCombined sources
Modified residuei69 – 691PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP30665.
PeptideAtlasiP30665.

PTM databases

iPTMnetiP30665.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MCM10P323543EBI-4326,EBI-5965
MCM2P294697EBI-4326,EBI-10533
MCM6P530915EBI-4326,EBI-10556
MCM7P381323EBI-4326,EBI-4300

Protein-protein interaction databases

BioGridi36196. 72 interactions.
DIPiDIP-2409N.
IntActiP30665. 30 interactions.
MINTiMINT-701903.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8041-933[»]
3JC5electron microscopy4.7041-933[»]
3JC6electron microscopy3.7041-933[»]
3JC7electron microscopy4.8041-933[»]
ProteinModelPortaliP30665.
SMRiP30665. Positions 177-838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini518 – 725208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi700 – 7034Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00790000123057.
InParanoidiP30665.
KOiK02212.
OMAiKNTIRIC.
OrthoDBiEOG7B5X4C.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008047. MCM_4.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01660. MCMPROTEIN4.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30665-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQQSSSPTK EDNNSSSPVV PNPDSVPPQL SSPALFYSSS SSQGDIYGRN
60 70 80 90 100
NSQNLSQGEG NIRAAIGSSP LNFPSSSQRQ NSDVFQSQGR QGRIRSSASA
110 120 130 140 150
SGRSRYHSDL RSDRALPTSS SSLGRNGQNR VHMRRNDIHT SDLSSPRRIV
160 170 180 190 200
DFDTRSGVNT LDTSSSSAPP SEASEPLRII WGTNVSIQEC TTNFRNFLMS
210 220 230 240 250
FKYKFRKILD EREEFINNTT DEELYYIKQL NEMRELGTSN LNLDARNLLA
260 270 280 290 300
YKQTEDLYHQ LLNYPQEVIS IMDQTIKDCM VSLIVDNNLD YDLDEIETKF
310 320 330 340 350
YKVRPYNVGS CKGMRELNPN DIDKLINLKG LVLRSTPVIP DMKVAFFKCN
360 370 380 390 400
VCDHTMAVEI DRGVIQEPAR CERIDCNEPN SMSLIHNRCS FADKQVIKLQ
410 420 430 440 450
ETPDFVPDGQ TPHSISLCVY DELVDSCRAG DRIEVTGTFR SIPIRANSRQ
460 470 480 490 500
RVLKSLYKTY VDVVHVKKVS DKRLDVDTST IEQELMQNKV DHNEVEEVRQ
510 520 530 540 550
ITDQDLAKIR EVAAREDLYS LLARSIAPSI YELEDVKKGI LLQLFGGTNK
560 570 580 590 600
TFTKGGRYRG DINILLCGDP STSKSQILQY VHKITPRGVY TSGKGSSAVG
610 620 630 640 650
LTAYITRDVD TKQLVLESGA LVLSDGGVCC IDEFDKMSDS TRSVLHEVME
660 670 680 690 700
QQTISIAKAG IITTLNARSS ILASANPIGS RYNPNLPVTE NIDLPPPLLS
710 720 730 740 750
RFDLVYLVLD KVDEKNDREL AKHLTNLYLE DKPEHISQDD VLPVEFLTMY
760 770 780 790 800
ISYAKEHIHP IITEAAKTEL VRAYVGMRKM GDDSRSDEKR ITATTRQLES
810 820 830 840 850
MIRLAEAHAK MKLKNVVELE DVQEAVRLIR SAIKDYATDP KTGKIDMNLV
860 870 880 890 900
QTGKSVIQRK LQEDLSREIM NVLKDQASDS MSFNELIKQI NEHSQDRVES
910 920 930
SDIQEALSRL QQEDKVIVLG EGVRRSVRLN NRV
Length:933
Mass (Da):105,003
Last modified:November 1, 1995 - v2
Checksum:i382D542AE38975E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14731 Genomic DNA. Translation: AAA86310.1.
Z49919 Genomic DNA. Translation: CAA90164.1.
Z71255 Genomic DNA. Translation: CAA95015.1.
Z15032 Genomic DNA. Translation: CAA78750.1.
BK006949 Genomic DNA. Translation: DAA11445.1.
PIRiS56050.
RefSeqiNP_015344.1. NM_001184116.1.

Genome annotation databases

EnsemblFungiiYPR019W; YPR019W; YPR019W.
GeneIDi856130.
KEGGisce:YPR019W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14731 Genomic DNA. Translation: AAA86310.1.
Z49919 Genomic DNA. Translation: CAA90164.1.
Z71255 Genomic DNA. Translation: CAA95015.1.
Z15032 Genomic DNA. Translation: CAA78750.1.
BK006949 Genomic DNA. Translation: DAA11445.1.
PIRiS56050.
RefSeqiNP_015344.1. NM_001184116.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8041-933[»]
3JC5electron microscopy4.7041-933[»]
3JC6electron microscopy3.7041-933[»]
3JC7electron microscopy4.8041-933[»]
ProteinModelPortaliP30665.
SMRiP30665. Positions 177-838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36196. 72 interactions.
DIPiDIP-2409N.
IntActiP30665. 30 interactions.
MINTiMINT-701903.

PTM databases

iPTMnetiP30665.

Proteomic databases

MaxQBiP30665.
PeptideAtlasiP30665.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR019W; YPR019W; YPR019W.
GeneIDi856130.
KEGGisce:YPR019W.

Organism-specific databases

EuPathDBiFungiDB:YPR019W.
SGDiS000006223. MCM4.

Phylogenomic databases

GeneTreeiENSGT00790000123057.
InParanoidiP30665.
KOiK02212.
OMAiKNTIRIC.
OrthoDBiEOG7B5X4C.

Enzyme and pathway databases

BioCyciYEAST:G3O-34179-MONOMER.
ReactomeiR-SCE-176974. Unwinding of DNA.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69052. Switching of origins to a post-replicative state.
R-SCE-69300. Removal of licensing factors from origins.

Miscellaneous databases

PROiP30665.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008047. MCM_4.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01660. MCMPROTEIN4.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Dalton S.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "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-574.
  4. "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 SER-52 AND SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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.
  6. "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.
  7. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  8. "Fission yeast cdc21+ belongs to a family of proteins involved in an early step of chromosome replication."
    Coxon A., Maundrell K., Kearsey S.E.
    Nucleic Acids Res. 20:5571-5577(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 571-646.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "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-52 AND SER-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCM4_YEAST
AccessioniPrimary (citable) accession number: P30665
Secondary accession number(s): D6W429
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8800 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

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.