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Protein

Minichromosome maintenance protein 5

Gene

MCM5

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; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. 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 bindingi416 – 4238ATPSequence analysis

GO - Molecular functioni

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

GO - Biological processi

  • chromatin silencing at telomere Source: SGD
  • DNA replication initiation Source: SGD
  • DNA strand elongation involved in DNA replication Source: Reactome
  • double-strand break repair via break-induced replication Source: SGD
  • establishment of chromatin silencing Source: SGD
  • negative regulation of chromatin silencing at telomere Source: SGD
  • nuclear DNA replication Source: SGD
  • pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: SGD
  • regulation of DNA-dependent DNA replication initiation 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-32373-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:
Minichromosome maintenance protein 5 (EC:3.6.4.12)
Alternative name(s):
Cell division control protein 46
Gene namesi
Name:MCM5
Synonyms:CDC46
Ordered Locus Names:YLR274W
ORF Names:L9328.1
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR274W.
SGDiS000004264. MCM5.

Subcellular locationi

  • Nucleus

  • Note: Mobilized from the cytoplasm to the nucleus as mitosis is completed. Remains in the nucleus until the initiation of the next round of replication.

GO - Cellular componenti

  • cytoplasm Source: SGD
  • DNA replication preinitiation complex Source: SGD
  • MCM complex Source: SGD
  • nuclear chromosome, telomeric region Source: SGD
  • nuclear pre-replicative complex 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
Mutagenesisi422 – 4221K → A: Loss of MCM2-7 complex helicase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 775775Minichromosome maintenance protein 5PRO_0000194111Add
BLAST

Proteomic databases

MaxQBiP29496.

PTM databases

iPTMnetiP29496.

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 CSM1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSM1P256512EBI-10549,EBI-22001
MCM3P242794EBI-10549,EBI-10541

Protein-protein interaction databases

BioGridi31542. 76 interactions.
DIPiDIP-2406N.
IntActiP29496. 78 interactions.
MINTiMINT-632183.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8051-775[»]
3JC5electron microscopy4.7051-775[»]
3JC6electron microscopy3.7051-775[»]
3JC7electron microscopy4.8051-775[»]
ProteinModelPortaliP29496.
SMRiP29496. Positions 2-693.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini366 – 573208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi548 – 5514Arginine finger

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi351 – 3566Poly-Glu

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00550000074928.
HOGENOMiHOG000224128.
InParanoidiP29496.
KOiK02209.
OMAiIVHDKCK.
OrthoDBiEOG7B5X4C.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008048. MCM5.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01661. MCMPROTEIN5.
SMARTiSM00350. 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.

P29496-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFDRPEIYS APVLQGESPN DDDNTEIIKS FKNFILEFRL DSQFIYRDQL
60 70 80 90 100
RNNILVKNYS LTVNMEHLIG YNEDIYKKLS DEPSDIIPLF ETAITQVAKR
110 120 130 140 150
ISILSRAQSA NNNDKDPENT SMDTDSLLLN SLPTFQLILN SNANQIPLRD
160 170 180 190 200
LDSEHVSKIV RLSGIIISTS VLSSRATYLS IMCRNCRHTT SITINNFNSI
210 220 230 240 250
TGNTVSLPRS CLSTIESESS MANESNIGDE STKKNCGPDP YIIIHESSKF
260 270 280 290 300
IDQQFLKLQE IPELVPVGEM PRNLTMTCDR YLTNKVIPGT RVTIVGIYSI
310 320 330 340 350
YNSKNGAGSG RSGGGNGGSG VAIRTPYIKI LGIQSDVETS SIWNSVTMFT
360 370 380 390 400
EEEEEEFLQL SRNPKLYEIL TNSIAPSIFG NEDIKKAIVC LLMGGSKKIL
410 420 430 440 450
PDGMRLRGDI NVLLLGDPGT AKSQLLKFVE KVSPIAVYTS GKGSSAAGLT
460 470 480 490 500
ASVQRDPMTR EFYLEGGAMV LADGGVVCID EFDKMRDEDR VAIHEAMEQQ
510 520 530 540 550
TISIAKAGIT TVLNSRTSVL AAANPIYGRY DDLKSPGDNI DFQTTILSRF
560 570 580 590 600
DMIFIVKDDH NEERDISIAN HVINIHTGNA NAMQNQQEEN GSEISIEKMK
610 620 630 640 650
RYITYCRLKC APRLSPQAAE KLSSNFVTIR KQLLINELES TERSSIPITI
660 670 680 690 700
RQLEAIIRIT ESLAKLELSP IAQERHVDEA IRLFQASTMD AASQDPIGGL
710 720 730 740 750
NQASGTSLSE IRRFEQELKR RLPIGWSTSY QTLRREFVDT HRFSQLALDK
760 770
ALYALEKHET IQLRHQGQNI YRSGV
Length:775
Mass (Da):86,411
Last modified:April 1, 1993 - v1
Checksum:i01D9DE208A091CF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09242 Unassigned DNA. Translation: AAA18027.1.
U17245 Genomic DNA. Translation: AAB67364.1.
BK006945 Genomic DNA. Translation: DAA09587.1.
PIRiA39631.
RefSeqiNP_013376.1. NM_001182161.1.

Genome annotation databases

EnsemblFungiiYLR274W; YLR274W; YLR274W.
GeneIDi850980.
KEGGisce:YLR274W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09242 Unassigned DNA. Translation: AAA18027.1.
U17245 Genomic DNA. Translation: AAB67364.1.
BK006945 Genomic DNA. Translation: DAA09587.1.
PIRiA39631.
RefSeqiNP_013376.1. NM_001182161.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8051-775[»]
3JC5electron microscopy4.7051-775[»]
3JC6electron microscopy3.7051-775[»]
3JC7electron microscopy4.8051-775[»]
ProteinModelPortaliP29496.
SMRiP29496. Positions 2-693.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31542. 76 interactions.
DIPiDIP-2406N.
IntActiP29496. 78 interactions.
MINTiMINT-632183.

PTM databases

iPTMnetiP29496.

Proteomic databases

MaxQBiP29496.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR274W; YLR274W; YLR274W.
GeneIDi850980.
KEGGisce:YLR274W.

Organism-specific databases

EuPathDBiFungiDB:YLR274W.
SGDiS000004264. MCM5.

Phylogenomic databases

GeneTreeiENSGT00550000074928.
HOGENOMiHOG000224128.
InParanoidiP29496.
KOiK02209.
OMAiIVHDKCK.
OrthoDBiEOG7B5X4C.

Enzyme and pathway databases

BioCyciYEAST:G3O-32373-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

PROiP29496.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008048. MCM5.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01661. MCMPROTEIN5.
SMARTiSM00350. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A group of interacting yeast DNA replication genes."
    Hennessy K.M., Lee A., Chen E., Botstein D.
    Genes Dev. 5:958-969(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(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-422.
  4. "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.
  5. "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.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "CDC46/MCM5, a yeast protein whose subcellular localization is cell cycle-regulated, is involved in DNA replication at autonomously replicating sequences."
    Chen Y., Hennessy K.M., Botstein D., Tye B.-K.
    Proc. Natl. Acad. Sci. U.S.A. 89:10459-10463(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF CDC46 WITH MCM5.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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.

Entry informationi

Entry nameiMCM5_YEAST
AccessioniPrimary (citable) accession number: P29496
Secondary accession number(s): D6VYS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 6, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 10300 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. 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.