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P24279 (MCM3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA replication licensing factor MCM3

EC=3.6.4.12
Alternative name(s):
Minichromosome maintenance protein 3
Gene names
Name:MCM3
Ordered Locus Names:YEL032W
ORF Names:SYGP-ORF23
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length971 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.7 Ref.8 Ref.11

Subcellular location

Nucleus.

Miscellaneous

Present with 35100 molecules/cell in log phase SD medium.

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.

Sequence similarities

Belongs to the MCM family.

Contains 1 MCM domain.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 12480933. Source: GOC

DNA duplex unwinding

Inferred from direct assay Ref.5. Source: GOC

DNA replication initiation

Inferred from mutant phenotype PubMed 12060653. Source: SGD

DNA strand elongation involved in DNA replication

Inferred from mutant phenotype PubMed 10834843. Source: SGD

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype PubMed 19064704. Source: SGD

chromatin silencing at telomere

Inferred from mutant phenotype PubMed 19064704. Source: SGD

double-strand break repair via break-induced replication

Inferred from mutant phenotype PubMed 20516198. Source: SGD

nuclear cell cycle DNA replication

Inferred from mutant phenotype PubMed 10834843. Source: SGD

pre-replicative complex assembly involved in nuclear cell cycle DNA replication

Inferred from direct assay PubMed 16824194. Source: SGD

   Cellular_componentDNA replication preinitiation complex

Inferred from physical interaction PubMed 9554851. Source: SGD

MCM complex

Inferred from direct assay PubMed 12480933. Source: SGD

cytoplasm

Inferred from direct assay PubMed 10704410. Source: SGD

nuclear pre-replicative complex

Inferred from direct assay PubMed 16824194PubMed 9335335. Source: SGD

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10704410. Source: SGD

replication fork protection complex

Inferred from direct assay PubMed 16531994. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA replication origin binding

Inferred from direct assay PubMed 11756674PubMed 16824194. Source: SGD

chromatin binding

Inferred from direct assay PubMed 9554851. Source: SGD

protein binding

Inferred from physical interaction PubMed 12480933Ref.11PubMed 16429126PubMed 21179020PubMed 23267104. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CSM1P256512EBI-10541,EBI-22001
MCM5P294964EBI-10541,EBI-10549

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 971971DNA replication licensing factor MCM3
PRO_0000194099

Regions

Domain359 – 566208MCM
Nucleotide binding409 – 4168ATP Potential
Motif541 – 5444Arginine finger

Amino acid modifications

Modified residue7611Phosphoserine Ref.12
Modified residue7771Phosphoserine Ref.4
Modified residue7811Phosphoserine Ref.4 Ref.12
Modified residue8681Phosphothreonine Ref.3

Experimental info

Mutagenesis4151K → 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. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P24279 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 43DD4DACAF4456DC

FASTA971107,518
        10         20         30         40         50         60 
MEGSTGFDGD ATTFFAPDAV FGDRVRRFQE FLDTFTSYRD SVRSIQVYNS NNAANYNDDQ 

        70         80         90        100        110        120 
DDADERDLLG DDDGDDLEKE KKAASSTSLN ILPHRIIISL DDLREFDRSF WSGILVEPAY 

       130        140        150        160        170        180 
FIPPAEKALT DLADSMDDVP HPNASAVSSR HPWKLSFKGS FGAHALSPRT LTAQHLNKLV 

       190        200        210        220        230        240 
SVEGIVTKTS LVRPKLIRSV HYAAKTGRFH YRDYTDATTT LTTRIPTPAI YPTEDTEGNK 

       250        260        270        280        290        300 
LTTEYGYSTF IDHQRITVQE MPEMAPAGQL PRSIDVILDD DLVDKTKPGD RVNVVGVFKS 

       310        320        330        340        350        360 
LGAGGMNQSN SNTLIGFKTL ILGNTVYPLH ARSTGVAARQ MLTDFDIRNI NKLSKKKDIF 

       370        380        390        400        410        420 
DILSQSLAPS IYGHDHIKKA ILLMLMGGVE KNLENGSHLR GDINILMVGD PSTAKSQLLR 

       430        440        450        460        470        480 
FVLNTASLAI ATTGRGSSGV GLTAAVTTDR ETGERRLEAG AMVLADRGVV CIDEFDKMTD 

       490        500        510        520        530        540 
VDRVAIHEVM EQQTVTIAKA GIHTTLNARC SVIAAANPVF GQYDVNRDPH QNIALPDSLL 

       550        560        570        580        590        600 
SRFDLLFVVT DDINEIRDRS ISEHVLRTHR YLPPGYLEGE PVRERLNLSL AVGEDADINP 

       610        620        630        640        650        660 
EEHSNSGAGV ENEGEDDEDH VFEKFNPLLQ AGAKLAKNKG NYNGTEIPKL VTIPFLRKYV 

       670        680        690        700        710        720 
QYAKERVIPQ LTQEAINVIV KNYTDLRNDD NTKKSPITAR TLETLIRLAT AHAKVRLSKT 

       730        740        750        760        770        780 
VNKVDAKVAA NLLRFALLGE DIGNDIDEEE SEYEEALSKR SPQKSPKKRQ RVRQPASNSG 

       790        800        810        820        830        840 
SPIKSTPRRS TASSVNATPS SARRILRFQD DEQNAGEDDN DIMSPLPADE EAELQRRLQL 

       850        860        870        880        890        900 
GLRVSPRRRE HLHAPEEGSS GPLTEVGTPR LPNVSSAGQD DEQQQSVISF DNVEPGTIST 

       910        920        930        940        950        960 
GRLSLISGII ARLMQTEIFE EESYPVASLF ERINEELPEE EKFSAQEYLA GLKIMSDRNN 

       970 
LMVADDKVWR V 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53540 Genomic DNA. Translation: CAA37616.1.
U18779 Genomic DNA. Translation: AAB65010.1.
BK006939 Genomic DNA. Translation: DAA07621.1.
PIRA36376.
RefSeqNP_010882.1. NM_001178847.1.

3D structure databases

ProteinModelPortalP24279.
SMRP24279. Positions 96-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36697. 51 interactions.
DIPDIP-2407N.
IntActP24279. 30 interactions.
MINTMINT-699197.
STRING4932.YEL032W.

Proteomic databases

MaxQBP24279.
PaxDbP24279.
PeptideAtlasP24279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL032W; YEL032W; YEL032W.
GeneID856680.
KEGGsce:YEL032W.

Organism-specific databases

CYGDYEL032w.
SGDS000000758. MCM3.

Phylogenomic databases

eggNOGCOG1241.
GeneTreeENSGT00550000075022.
HOGENOMHOG000224126.
KOK02541.
OMAVLRTHRY.
OrthoDBEOG7B5X4C.

Enzyme and pathway databases

BioCycYEAST:G3O-30154-MONOMER.
ReactomeREACT_190740. Cell Cycle.

Gene expression databases

GenevestigatorP24279.

Family and domain databases

Gene3D2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProIPR003593. 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]
PfamPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSPR01657. MCMFAMILY.
PR01659. MCMPROTEIN3.
SMARTSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982707.
PROP24279.

Entry information

Entry nameMCM3_YEAST
AccessionPrimary (citable) accession number: P24279
Secondary accession number(s): D3DLL7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families