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Protein

DNA replication licensing factor MCM3

Gene

MCM3

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. Necessary for cell growth.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi409 – 4168ATPSequence 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 silent mating-type cassette Source: SGD
  • chromatin silencing at telomere Source: SGD
  • DNA duplex unwinding Source: GOC
  • DNA replication initiation Source: SGD
  • DNA strand elongation 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

DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30154-MONOMER.
ReactomeiREACT_289355. Removal of licensing factors from origins.
REACT_303130. Unwinding of DNA.
REACT_342755. Switching of origins to a post-replicative state.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM3 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance protein 3
Gene namesi
Name:MCM3
Ordered Locus Names:YEL032W
ORF Names:SYGP-ORF23
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

CYGDiYEL032w.
EuPathDBiFungiDB:YEL032W.
SGDiS000000758. MCM3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • DNA replication preinitiation complex Source: SGD
  • MCM complex 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
Mutagenesisi415 – 4151K → A: No effect on MCM2-7 complex helicase activity. Loss of MCM2-7 complex helicase activity; when associated with MCM5 A-422. Reduces MCM2-7 complex helicase activity; when asscociated with MCM2 A-549. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 971971DNA replication licensing factor MCM3PRO_0000194099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei761 – 7611Phosphoserine1 Publication
Modified residuei777 – 7771Phosphoserine1 Publication
Modified residuei781 – 7811Phosphoserine2 Publications
Modified residuei868 – 8681Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP24279.
PaxDbiP24279.
PeptideAtlasiP24279.

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-10541,EBI-22001
MCM5P294964EBI-10541,EBI-10549

Protein-protein interaction databases

BioGridi36697. 54 interactions.
DIPiDIP-2407N.
IntActiP24279. 30 interactions.
MINTiMINT-699197.
STRINGi4932.YEL032W.

Structurei

3D structure databases

ProteinModelPortaliP24279.
SMRiP24279. Positions 96-570, 656-737.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini359 – 566208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi541 – 5444Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00550000075022.
HOGENOMiHOG000224126.
InParanoidiP24279.
KOiK02541.
OMAiVLRTHRY.
OrthoDBiEOG7B5X4C.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008046. Mcm3.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
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.
PR01659. MCMPROTEIN3.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24279-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGSTGFDGD ATTFFAPDAV FGDRVRRFQE FLDTFTSYRD SVRSIQVYNS
60 70 80 90 100
NNAANYNDDQ DDADERDLLG DDDGDDLEKE KKAASSTSLN ILPHRIIISL
110 120 130 140 150
DDLREFDRSF WSGILVEPAY FIPPAEKALT DLADSMDDVP HPNASAVSSR
160 170 180 190 200
HPWKLSFKGS FGAHALSPRT LTAQHLNKLV SVEGIVTKTS LVRPKLIRSV
210 220 230 240 250
HYAAKTGRFH YRDYTDATTT LTTRIPTPAI YPTEDTEGNK LTTEYGYSTF
260 270 280 290 300
IDHQRITVQE MPEMAPAGQL PRSIDVILDD DLVDKTKPGD RVNVVGVFKS
310 320 330 340 350
LGAGGMNQSN SNTLIGFKTL ILGNTVYPLH ARSTGVAARQ MLTDFDIRNI
360 370 380 390 400
NKLSKKKDIF DILSQSLAPS IYGHDHIKKA ILLMLMGGVE KNLENGSHLR
410 420 430 440 450
GDINILMVGD PSTAKSQLLR FVLNTASLAI ATTGRGSSGV GLTAAVTTDR
460 470 480 490 500
ETGERRLEAG AMVLADRGVV CIDEFDKMTD VDRVAIHEVM EQQTVTIAKA
510 520 530 540 550
GIHTTLNARC SVIAAANPVF GQYDVNRDPH QNIALPDSLL SRFDLLFVVT
560 570 580 590 600
DDINEIRDRS ISEHVLRTHR YLPPGYLEGE PVRERLNLSL AVGEDADINP
610 620 630 640 650
EEHSNSGAGV ENEGEDDEDH VFEKFNPLLQ AGAKLAKNKG NYNGTEIPKL
660 670 680 690 700
VTIPFLRKYV QYAKERVIPQ LTQEAINVIV KNYTDLRNDD NTKKSPITAR
710 720 730 740 750
TLETLIRLAT AHAKVRLSKT VNKVDAKVAA NLLRFALLGE DIGNDIDEEE
760 770 780 790 800
SEYEEALSKR SPQKSPKKRQ RVRQPASNSG SPIKSTPRRS TASSVNATPS
810 820 830 840 850
SARRILRFQD DEQNAGEDDN DIMSPLPADE EAELQRRLQL GLRVSPRRRE
860 870 880 890 900
HLHAPEEGSS GPLTEVGTPR LPNVSSAGQD DEQQQSVISF DNVEPGTIST
910 920 930 940 950
GRLSLISGII ARLMQTEIFE EESYPVASLF ERINEELPEE EKFSAQEYLA
960 970
GLKIMSDRNN LMVADDKVWR V
Length:971
Mass (Da):107,518
Last modified:March 1, 1992 - v1
Checksum:i43DD4DACAF4456DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53540 Genomic DNA. Translation: CAA37616.1.
U18779 Genomic DNA. Translation: AAB65010.1.
BK006939 Genomic DNA. Translation: DAA07621.1.
PIRiA36376.
RefSeqiNP_010882.1. NM_001178847.1.

Genome annotation databases

EnsemblFungiiYEL032W; YEL032W; YEL032W.
GeneIDi856680.
KEGGisce:YEL032W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53540 Genomic DNA. Translation: CAA37616.1.
U18779 Genomic DNA. Translation: AAB65010.1.
BK006939 Genomic DNA. Translation: DAA07621.1.
PIRiA36376.
RefSeqiNP_010882.1. NM_001178847.1.

3D structure databases

ProteinModelPortaliP24279.
SMRiP24279. Positions 96-570, 656-737.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36697. 54 interactions.
DIPiDIP-2407N.
IntActiP24279. 30 interactions.
MINTiMINT-699197.
STRINGi4932.YEL032W.

Proteomic databases

MaxQBiP24279.
PaxDbiP24279.
PeptideAtlasiP24279.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL032W; YEL032W; YEL032W.
GeneIDi856680.
KEGGisce:YEL032W.

Organism-specific databases

CYGDiYEL032w.
EuPathDBiFungiDB:YEL032W.
SGDiS000000758. MCM3.

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00550000075022.
HOGENOMiHOG000224126.
InParanoidiP24279.
KOiK02541.
OMAiVLRTHRY.
OrthoDBiEOG7B5X4C.

Enzyme and pathway databases

BioCyciYEAST:G3O-30154-MONOMER.
ReactomeiREACT_289355. Removal of licensing factors from origins.
REACT_303130. Unwinding of DNA.
REACT_342755. Switching of origins to a post-replicative state.

Miscellaneous databases

NextBioi982707.
PROiP24279.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008046. Mcm3.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
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.
PR01659. MCMPROTEIN3.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The phenotype of the minichromosome maintenance mutant mcm3 is characteristic of mutants defective in DNA replication."
    Gibson S.T., Suroski R.T., Tye B.K.
    Mol. Cell. Biol. 10:5707-5720(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "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-868, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  4. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777 AND SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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-415.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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.
  8. "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.
  9. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "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.
  12. "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-761 AND SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCM3_YEAST
AccessioniPrimary (citable) accession number: P24279
Secondary accession number(s): D3DLL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 24, 2015
This is version 152 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 35100 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

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

External Data

Dasty 3

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 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.