P53091 (MCM6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA replication licensing factor MCM6
EC=3.6.4.12

Alternative name(s):
Minichromosome maintenance protein 6

Gene names

Name:	MCM6
Ordered Locus Names:	YGL201C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1017 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. Required for the entry in S phase and for cell division. 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 MCM10. Ref.8
Subcellular location	Nucleus Potential.
Miscellaneous	Present with 13400 molecules/cell in log phase SD medium. Ref.9 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	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 strand elongation involved in DNA replication Inferred from mutant phenotype. Source: SGD DNA unwinding involved in replication Inferred from direct assay. Source: SGD DNA-dependent DNA replication initiation Inferred from physical interaction. Source: SGD S phase of mitotic cell cycle Inferred from mutant phenotype. Source: SGD double-strand break repair via break-induced replication Inferred from mutant phenotype. Source: SGD pre-replicative complex assembly Inferred from direct assay. Source: SGD
Cellular component	DNA replication preinitiation complex Inferred from direct assay. Source: SGD MCM complex Inferred from direct assay. Source: SGD cytoplasm Inferred from direct assay. Source: SGD pre-replicative complex Inferred from direct assay. Source: SGD replication fork protection complex Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA replication origin binding Inferred from direct assay. Source: SGD four-way junction helicase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction Ref.8. Source: IntAct single-stranded DNA-dependent ATPase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MCM10	P32354	3	EBI-10556,EBI-5965
MCM4	P30665	2	EBI-10556,EBI-4326

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1017	1017	DNA replication licensing factor MCM6		PRO_0000194117
Regions
	Domain	525 – 732	208	MCM
	Nucleotide binding	575 – 582	8	ATP Potential
	Motif	707 – 710	4	Arginine finger
Amino acid modifications
	Modified residue	31	1	Phosphoserine Ref.11
	Modified residue	78	1	Phosphoserine Ref.11
	Modified residue	249	1	Phosphoserine Ref.11
	Modified residue	372	1	Phosphoserine Ref.11
	Modified residue	766	1	Phosphothreonine Ref.10
	Modified residue	1016	1	Phosphoserine Ref.11
	Modified residue	1017	1	Phosphoserine Ref.11
Experimental info
	Mutagenesis	581	1	K → A: Loss of MCM2-7 complex helicase activity. Ref.3
	Sequence conflict	179	1	P → A in CAA96913. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P53091 [UniParc]. Last modified October 5, 2010. Version 2. Checksum: 03AB793134E64A50	FASTA	1,017	112,978
	10 20 30 40 50 60 MSSPFPADTP SSNRPSNSSP PPSSIGAGFG SSSGLDSQIG SRLHFPSSSQ PHVSNSQTGP 70 80 90 100 110 120 FVNDSTQFSS QRLQTDGSAT NDMEGNEPAR SFKSRALNHV KKVDDVTGEK VREAFEQFLE 130 140 150 160 170 180 DFSVQSTDTG EVEKVYRAQI EFMKIYDLNT IYIDYQHLSM RENGALAMAI SEQYYRFLPF 190 200 210 220 230 240 LQKGLRRVVR KYAPELLNTS DSLKRSEGDE GQADEDEQQD DDMNGSSLPR DSGSSAAPGN 250 260 270 280 290 300 GTSAMATRSI TTSTSPEQTE RVFQISFFNL PTVHRIRDIR SEKIGSLLSI SGTVTRTSEV 310 320 330 340 350 360 RPELYKASFT CDMCRAIVDN VEQSFKYTEP TFCPNPSCEN RAFWTLNVTR SRFLDWQKVR 370 380 390 400 410 420 IQENANEIPT GSMPRTLDVI LRGDSVERAK PGDRCKFTGV EIVVPDVTQL GLPGVKPSST 430 440 450 460 470 480 LDTRGISKTT EGLNSGVTGL RSLGVRDLTY KISFLACHVI SIGSNIGASS PDANSNNRET 490 500 510 520 530 540 ELQMAANLQA NNVYQDNERD QEVFLNSLSS DEINELKEMV KDEHIYDKLV RSIAPAVFGH 550 560 570 580 590 600 EAVKKGILLQ MLGGVHKSTV EGIKLRGDIN ICVVGDPSTS KSQFLKYVVG FAPRSVYTSG 610 620 630 640 650 660 KASSAAGLTA AVVRDEEGGD YTIEAGALML ADNGICCIDE FDKMDISDQV AIHEAMEQQT 670 680 690 700 710 720 ISIAKAGIHA TLNARTSILA AANPVGGRYN RKLSLRGNLN MTAPIMSRFD LFFVILDDCN 730 740 750 760 770 780 EKIDTELASH IVDLHMKRDE AIEPPFSAEQ LRRYIKYART FKPILTKEAR SYLVEKYKEL 790 800 810 820 830 840 RKDDAQGFSR SSYRITVRQL ESMIRLSEAI ARANCVDEIT PSFIAEAYDL LRQSIIRVDV 850 860 870 880 890 900 DDVEMDEEFD NIESQSHAAS GNNDDNDDGT GSGVITSEPP ADIEEGQSEA TARPGTSEKK 910 920 930 940 950 960 KTTVTYDKYV SMMNMIVRKI AEVDREGAEE LTAVDIVDWY LLQKENDLGS LAEYWEERRL 970 980 990 1000 1010 AFKVIKRLVK DRILMEIHGT RHNLRDLENE ENENNKTVYV IHPNCEVLDQ LEPQDSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the Saccharomyces cerevisiae MCM6 gene." Duina A.A., Winston F. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The Mcm2-7 complex has in vitro helicase activity." Bochman M.L., Schwacha A. Mol. Cell 31:287-293(2008) [PubMed: 18657510] [Abstract] Cited for: RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7 COMPLEX, MUTAGENESIS OF LYS-581.
[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: 19896182] [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: 19910535] [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]	"Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily." Iraqui I., Vissers S., Cartiaux M., Urrestarazu A. Mol. Gen. Genet. 257:238-248(1998) [PubMed: 9491083] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-1017. Strain: Sigma 1278B.
[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: 9154825] [Abstract] Cited for: INTERACTION WITH MCM10.
[9]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-766, MASS SPECTROMETRY. Strain: ADR376.
[11]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-78; SER-249; SER-372; SER-1016 AND SER-1017, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY258324 Genomic DNA. Translation: AAO89010.1. Z72723 Genomic DNA. Translation: CAA96913.1. Y13624 Genomic DNA. Translation: CAA73947.1. BK006941 Genomic DNA. Translation: DAA07914.1.
PIR	S64219.
RefSeq	NP_011314.2. NM_001181066.1.
3D structure databases
ProteinModelPortal	P53091.
SMR	P53091. Positions 897-1009.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1294N.
IntAct	P53091. 47 interactions.
MINT	MINT-397018.
STRING	P53091.
Proteomic databases
PeptideAtlas	P53091.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL201C; YGL201C; YGL201C.
GeneID	852673.
KEGG	sce:YGL201C.
Organism-specific databases
SGD	S000003169. MCM6.
Phylogenomic databases
eggNOG	fuNOG04804.
GeneTree	EFGT00050000003095.
HOGENOM	HBG546212.
OMA	FLKYICS.
OrthoDB	EOG4CNV06.
Enzyme and pathway databases
Reactome	REACT_101785. DNA Replication. REACT_108233. Cell Cycle, Mitotic.
Gene expression databases
ArrayExpress	P53091.
Genevestigator	P53091.
GermOnline	YGL201C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008049. MCM_6. IPR018525. MCM_CS. IPR001208. MCM_DNA-dep_ATPase. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K02542.
Pfam	PF00493. MCM. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01662. MCMPROTEIN6.
SMART	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...

Entry information

Entry name

MCM6_YEAST

Accession

Primary (citable) accession number: P53091
Secondary accession number(s): D6VTV3, Q870M9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 5, 2010
Last modified:	December 14, 2011
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program