P38132 (MCM7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA replication licensing factor MCM7
EC=3.6.4.12

Alternative name(s):
Cell division control protein 47
Minichromosome maintenance protein 7

Gene names

Name:	MCM7
Synonyms:	CDC47
Ordered Locus Names:	YBR202W
ORF Names:	YBR1441

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	845 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. Ref.6 Ref.7
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 and MCM10. Ref.6 Ref.7 Ref.8 Ref.12
Subcellular location	Cytoplasm. Nucleus Ref.10.
Miscellaneous	Present with 166 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. 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.
Sequence similarities	Belongs to the MCM family. Contains 1 MCM domain.

Ontologies

Keywords
Biological process	Cell cycle DNA replication
Cellular component	Cytoplasm 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	DNA replication initiation Inferred from mutant phenotype PubMed 10783164PubMed 2044962. Source: SGD DNA strand elongation involved in DNA replication Inferred from mutant phenotype PubMed 10783164PubMed 10834843. Source: SGD DNA unwinding involved in replication Inferred from direct assay PubMed 13679365PubMed 15723534. Source: SGD S phase of mitotic cell cycle Inferred from mutant phenotype PubMed 10834843PubMed 2044962. 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 regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 12738768. Source: SGD
Cellular_component	DNA replication preinitiation complex Inferred from direct assay PubMed 9554851. Source: SGD MCM complex Inferred from direct assay PubMed 12480933. Source: SGD cytoplasm Inferred from direct assay PubMed 10704410Ref.1. Source: SGD pre-replicative complex Inferred from direct assay PubMed 16824194PubMed 9335335. Source: SGD replication fork protection complex Inferred from direct assay PubMed 16531994. Source: SGD
Molecular_function	ATP binding Inferred from direct assay PubMed 12480933. Source: SGD DNA replication origin binding Inferred from direct assay PubMed 11756674PubMed 16824194PubMed 9288745. Source: SGD chromatin binding Inferred from direct assay PubMed 9159120PubMed 9288745. Source: SGD four-way junction helicase activity Inferred from direct assay PubMed 13679365. Source: SGD single-stranded DNA-dependent ATPase activity Inferred from direct assay PubMed 15723534. Source: SGD transcription cofactor activity Inferred from direct assay PubMed 12738768. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSM1	P25651	3	EBI-4300,EBI-22001
ERG26	P53199	2	EBI-4300,EBI-6514
MCM4	P30665	2	EBI-4300,EBI-4326

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 845	845	DNA replication licensing factor MCM7		PRO_0000194124
Regions
	Domain	410 – 617	208	MCM
	Nucleotide binding	460 – 467	8	ATP Potential
	Motif	592 – 595	4	Arginine finger
Amino acid modifications
	Modified residue	811	1	Phosphothreonine Ref.9 Ref.13 Ref.14
	Modified residue	816	1	Phosphoserine Ref.14
	Modified residue	819	1	Phosphoserine Ref.9 Ref.14
Experimental info
	Mutagenesis	466	1	K → A: Loss of MCM2-7 complex helicase activity. Ref.5
	Sequence conflict	552	1	G → V in CAA79689. Ref.2
	Sequence conflict	552	1	G → V in CAA85166. Ref.3
	Sequence conflict	556 – 558	3	TLN → NPG in CAA79689. Ref.2
	Sequence conflict	556 – 558	3	TLN → NPG in CAA85166. Ref.3
	Sequence conflict	574	1	Y → I in CAA79689. Ref.2
	Sequence conflict	574	1	Y → I in CAA85166. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P38132 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: ADA66C719D96DB4A	FASTA	845	94,943
	10 20 30 40 50 60 MSAALPSIQL PVDYNNLFNE ITDFLVTFKQ DTLSSDATRN ENEDENLDAE NIEQHLLEKG 70 80 90 100 110 120 PKYMAMLQKV ANRELNSVII DLDDILQYQN EKFLQGTQAD DLVSAIQQNA NHFTELFCRA 130 140 150 160 170 180 IDNNMPLPTK EIDYKDDVLD VILNQRRLRN ERMLSDRTNE IRSENLMDTT MDPPSSMNDA 190 200 210 220 230 240 LREVVEDETE LFPPNLTRRY FLYFKPLSQN CARRYRKKAI SSKPLSVRQI KGDFLGQLIT 250 260 270 280 290 300 VRGIITRVSD VKPAVEVIAY TCDQCGYEVF QEVNSRTFTP LSECTSEECS QNQTKGQLFM 310 320 330 340 350 360 STRASKFSAF QECKIQELSQ QVPVGHIPRS LNIHVNGTLV RSLSPGDIVD VTGIFLPAPY 370 380 390 400 410 420 TGFKALKAGL LTETYLEAQF VRQHKKKFAS FSLTSDVEER VMELITSGDV YNRLAKSIAP 430 440 450 460 470 480 EIYGNLDVKK ALLLLLVGGV DKRVGDGMKI RGDINVCLMG DPGVAKSQLL KAICKISPRG 490 500 510 520 530 540 VYTTGKGSSG VGLTAAVMKD PVTDEMILEG GALVLADNGI CCIDEFDKMD ESDRTAIHEV 550 560 570 580 590 600 MEQQTISISK AGINTTLNAR TSILAAANPL YGRYNPRLSP LDNINLPAAL LSRFDILFLM 610 620 630 640 650 660 LDIPSRDDDE KLAEHVTYVH MHNKQPDLDF TPVEPSKMRE YIAYAKTKRP VMSEAVNDYV 670 680 690 700 710 720 VQAYIRLRQD SKREMDSKFS FGQATPRTLL GIIRLSQALA KLRLADMVDI DDVEEALRLV 730 740 750 760 770 780 RVSKESLYQE TNKSKEDESP TTKIFTIIKK MLQETGKNTL SYENIVKTVR LRGFTMLQLS 790 800 810 820 830 840 NCIQEYSYLN VWHLINEGNT LKFVDDGTMD TDQEDSLVST PKLAPQTTAS ANVSAQDSDI DLQDA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cell cycle-regulated nuclear import and export of Cdc47, a protein essential for initiation of DNA replication in budding yeast." Dalton S., Whitbread L. Proc. Natl. Acad. Sci. U.S.A. 92:2514-2518(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 12.8 kb segment, on the right arm of chromosome II from Saccharomyces cerevisiae including part of the DUR1,2 gene, contains five putative new genes." Bussereau F., Mallet L., Gaillon L., Jacquet M. Yeast 9:797-806(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 552; 556-558 AND 574. Strain: ATCC 204508 / S288c.
[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-466.
[6]	"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.
[7]	"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.
[8]	"A lesion in the DNA replication initiation factor Mcm10 induces pausing of elongation forks through chromosomal replication origins in Saccharomyces cerevisiae." Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K. Mol. Cell. Biol. 17:3261-3271(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MCM10.
[9]	"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 THR-811 AND SER-819, MASS SPECTROMETRY. Strain: 2124.
[10]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]	"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].
[12]	"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.
[13]	"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-811, MASS SPECTROMETRY. Strain: ADR376.
[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-811; SER-816 AND SER-819, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14730 Genomic DNA. Translation: AAA86309.1. Z21487 Genomic DNA. Translation: CAA79689.1. Z36071 Genomic DNA. Translation: CAA85166.1. BK006936 Genomic DNA. Translation: DAA07320.2.
PIR	S34027.
RefSeq	NP_009761.4. NM_001178550.4.
3D structure databases
ProteinModelPortal	P38132.
SMR	P38132. Positions 131-355, 409-729.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2408N.
IntAct	P38132. 11 interactions.
MINT	MINT-637194.
STRING	4932.YBR202W.
Proteomic databases
PaxDb	P38132.
PeptideAtlas	P38132.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR202W; YBR202W; YBR202W.
GeneID	852501.
KEGG	sce:YBR202W. sce:YBR207W.
Organism-specific databases
CYGD	YBR202w.
SGD	S000000406. MCM7.
Phylogenomic databases
eggNOG	COG1241.
GeneTree	ENSGT00670000098113.
KO	K02210.
OMA	TFTSARN.
OrthoDB	EOG4H1F3W.
Enzyme and pathway databases
Reactome	REACT_101785. DNA Replication. REACT_118473. Cell Cycle.
Gene expression databases
Genevestigator	P38132.
GermOnline	YBR202W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.40.50.140. 2 hits.
InterPro	IPR003593. AAA+_ATPase. IPR008050. MCM7. IPR018525. MCM_CS. IPR001208. MCM_DNA-dep_ATPase. IPR012340. NA-bd_OB-fold. [Graphical view]
PANTHER	PTHR11630:SF26. PTHR11630:SF26. 1 hit.
Pfam	PF00493. MCM. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01663. MCMPROTEIN7.
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	971507.

Entry information

Entry name

MCM7_YEAST

Accession

Primary (citable) accession number: P38132
Secondary accession number(s): D6VQK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 129 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program