DNA replication licensing factor MCM3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P24279 (MCM3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	971 AA.
Sequence status	Complete.
Protein existence	Evidence 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.4 Ref.5
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.4 Ref.5 Ref.9
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 process	DNA replication
Cellular component	Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay PubMed 12480933. Source: GOC DNA duplex unwinding Inferred from direct assay Ref.3. 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 S phase of mitotic cell cycle 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 pre-replicative complex assembly Inferred from direct assay PubMed 16824194. Source: SGD
Cellular_component	DNA 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 PubMed 11914276. Source: SGD pre-replicative complex Inferred from direct assay PubMed 16824194 PubMed 9335335. Source: SGD replication fork protection complex Inferred from direct assay PubMed 16531994. Source: SGD
Molecular_function	ATP 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 11756674 PubMed 16824194. Source: SGD chromatin binding Inferred from direct assay PubMed 9554851. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSM1	P25651	2	EBI-10541,EBI-22001
MCM5	P29496	4	EBI-10541,EBI-10549

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 971

971

DNA replication licensing factor MCM3

PRO_0000194099

Regions

Domain

359 – 566

208

MCM

Nucleotide binding

409 – 416

ATP Potential

Motif

541 – 544

Arginine finger

Amino acid modifications

Modified residue

227

Phosphothreonine Ref.14

Modified residue

777

Phosphoserine Ref.7 Ref.12 Ref.13 Ref.14

Modified residue

779

Phosphoserine Ref.13

Modified residue

781

Phosphoserine Ref.7 Ref.12 Ref.13 Ref.14

Modified residue

786

Phosphothreonine Ref.13

Modified residue

790

Phosphoserine Ref.13

Modified residue

791

Phosphothreonine Ref.13

Modified residue

794

Phosphoserine Ref.7 Ref.13 Ref.14

Modified residue

800

Phosphoserine Ref.7

Modified residue

801

Phosphoserine Ref.13

Modified residue

845

Phosphoserine Ref.10 Ref.14

Modified residue

868

Phosphothreonine Ref.11

Experimental info

Mutagenesis

415

K → 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.3

Sequences

Sequence

Length

Mass (Da)

Tools

P24279 [UniParc].

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

FASTA

971

107,518

        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' referencesShow '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. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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-415.
[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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777; SER-781; SER-794 AND SER-800, MASS SPECTROMETRY. Strain: 2124.
[8]	"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].
[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.
[10]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-845, MASS SPECTROMETRY. Strain: YAL6B.
[11]	"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, MASS SPECTROMETRY. Strain: ADR376.
[12]	"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, MASS SPECTROMETRY.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777; SER-779; SER-781; THR-786; SER-790; THR-791; SER-794 AND SER-801, MASS SPECTROMETRY.
[14]	"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-227; SER-777; SER-781; SER-794 AND SER-845, MASS SPECTROMETRY.
+	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.
PIR	A36376.
RefSeq	NP_010882.1. NM_001178847.1.
3D structure databases
ProteinModelPortal	P24279.
SMR	P24279. Positions 96-569.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2407N.
IntAct	P24279. 30 interactions.
MINT	MINT-699197.
STRING	4932.YEL032W.
Proteomic databases
PaxDb	P24279.
PeptideAtlas	P24279.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YEL032W; YEL032W; YEL032W.
GeneID	856680.
KEGG	sce:YEL032W.
Organism-specific databases
CYGD	YEL032w.
SGD	S000000758. MCM3.
Phylogenomic databases
eggNOG	COG1241.
GeneTree	ENSGT00550000075022.
HOGENOM	HOG000224126.
KO	K02541.
OMA	LRTHRYL.
OrthoDB	EOG4J14HB.
Enzyme and pathway databases
Reactome	REACT_101785. DNA Replication. REACT_118473. Cell Cycle.
Gene expression databases
Genevestigator	P24279.
GermOnline	YEL032W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.40.50.140. 2 hits.
InterPro	IPR003593. AAA+_ATPase. IPR008046. Mcm3. IPR018525. MCM_CS. IPR001208. MCM_DNA-dep_ATPase. IPR012340. NA-bd_OB-fold. [Graphical view]
Pfam	PF00493. MCM. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01659. MCMPROTEIN3.
SMART	SM00382. AAA. 1 hit. SM00350. MCM. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
PROSITE	PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982707.

Entry information

Entry name

MCM3_YEAST

Accession

Primary (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:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome V

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents