P29496 (MCM5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Minichromosome maintenance protein 5
EC=3.6.4.12

Alternative name(s):
Cell division control protein 46

Gene names

Name:	MCM5
Synonyms:	CDC46
Ordered Locus Names:	YLR274W
ORF Names:	L9328.1

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	775 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; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. 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.9
Subcellular location	Nucleus. Note: Mobilized from the cytoplasm to the nucleus as mitosis is completed. Remains in the nucleus until the initiation of the next round of replication.
Miscellaneous	Present with 10300 molecules/cell in log phase SD medium. Ref.8 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	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-dependent DNA replication initiation Inferred from mutant phenotype. Source: SGD S phase of mitotic cell cycle Inferred from mutant phenotype Ref.1. Source: SGD chromatin silencing at telomere Inferred from mutant phenotype. Source: SGD double-strand break repair via break-induced replication Inferred from mutant phenotype. Source: SGD establishment of chromatin silencing Inferred from mutant phenotype. Source: SGD negative regulation of chromatin silencing at telomere Inferred from mutant phenotype. Source: SGD pre-replicative complex assembly Inferred from direct assay. Source: SGD regulation of DNA-dependent DNA replication initiation Inferred from mutant phenotype. Source: SGD
Cellular component	DNA replication preinitiation complex Inferred from physical interaction. Source: SGD MCM complex Inferred from direct assay. Source: SGD cytoplasm Inferred from direct assay. Source: SGD nuclear chromosome, telomeric region 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 chromatin binding Inferred from direct assay. Source: SGD helicase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.9. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSM1	P25651	2	EBI-10549,EBI-22001
MCM3	P24279	3	EBI-10549,EBI-10541

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 775	775	Minichromosome maintenance protein 5		PRO_0000194111
Regions
	Domain	366 – 573	208	MCM
	Nucleotide binding	416 – 423	8	ATP Potential
	Motif	548 – 551	4	Arginine finger
	Compositional bias	351 – 356	6	Poly-Glu
Amino acid modifications
	Modified residue	312	1	Phosphoserine Ref.10
	Modified residue	319	1	Phosphoserine Ref.10
Experimental info
	Mutagenesis	422	1	K → A: Loss of MCM2-7 complex helicase activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P29496 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 01D9DE208A091CF2	FASTA	775	86,411
	10 20 30 40 50 60 MSFDRPEIYS APVLQGESPN DDDNTEIIKS FKNFILEFRL DSQFIYRDQL RNNILVKNYS 70 80 90 100 110 120 LTVNMEHLIG YNEDIYKKLS DEPSDIIPLF ETAITQVAKR ISILSRAQSA NNNDKDPENT 130 140 150 160 170 180 SMDTDSLLLN SLPTFQLILN SNANQIPLRD LDSEHVSKIV RLSGIIISTS VLSSRATYLS 190 200 210 220 230 240 IMCRNCRHTT SITINNFNSI TGNTVSLPRS CLSTIESESS MANESNIGDE STKKNCGPDP 250 260 270 280 290 300 YIIIHESSKF IDQQFLKLQE IPELVPVGEM PRNLTMTCDR YLTNKVIPGT RVTIVGIYSI 310 320 330 340 350 360 YNSKNGAGSG RSGGGNGGSG VAIRTPYIKI LGIQSDVETS SIWNSVTMFT EEEEEEFLQL 370 380 390 400 410 420 SRNPKLYEIL TNSIAPSIFG NEDIKKAIVC LLMGGSKKIL PDGMRLRGDI NVLLLGDPGT 430 440 450 460 470 480 AKSQLLKFVE KVSPIAVYTS GKGSSAAGLT ASVQRDPMTR EFYLEGGAMV LADGGVVCID 490 500 510 520 530 540 EFDKMRDEDR VAIHEAMEQQ TISIAKAGIT TVLNSRTSVL AAANPIYGRY DDLKSPGDNI 550 560 570 580 590 600 DFQTTILSRF DMIFIVKDDH NEERDISIAN HVINIHTGNA NAMQNQQEEN GSEISIEKMK 610 620 630 640 650 660 RYITYCRLKC APRLSPQAAE KLSSNFVTIR KQLLINELES TERSSIPITI RQLEAIIRIT 670 680 690 700 710 720 ESLAKLELSP IAQERHVDEA IRLFQASTMD AASQDPIGGL NQASGTSLSE IRRFEQELKR 730 740 750 760 770 RLPIGWSTSY QTLRREFVDT HRFSQLALDK ALYALEKHET IQLRHQGQNI YRSGV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A group of interacting yeast DNA replication genes." Hennessy K.M., Lee A., Chen E., Botstein D. Genes Dev. 5:958-969(1991) [PubMed: 2044962] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [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: 18657510] [Abstract] Cited for: RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7 COMPLEX, MUTAGENESIS OF LYS-422.
[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]	"CDC46/MCM5, a yeast protein whose subcellular localization is cell cycle-regulated, is involved in DNA replication at autonomously replicating sequences." Chen Y., Hennessy K.M., Botstein D., Tye B.-K. Proc. Natl. Acad. Sci. U.S.A. 89:10459-10463(1992) [PubMed: 1438234] [Abstract] Cited for: IDENTIFICATION OF CDC46 WITH MCM5.
[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: 14562106] [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: 15023545] [Abstract] Cited for: INTERACTION WITH CSM1.
[10]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-319, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U09242 Unassigned DNA. Translation: AAA18027.1. U17245 Genomic DNA. Translation: AAB67364.1. BK006945 Genomic DNA. Translation: DAA09587.1.
PIR	A39631.
RefSeq	NP_013376.1. NM_001182161.1.
3D structure databases
ProteinModelPortal	P29496.
SMR	P29496. Positions 25-692.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2406N.
IntAct	P29496. 80 interactions.
MINT	MINT-632183.
STRING	P29496.
Proteomic databases
PeptideAtlas	P29496.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR274W; YLR274W; YLR274W.
GeneID	850980.
KEGG	sce:YLR274W.
NMPDR	fig|4932.3.peg.4391.
Organism-specific databases
CYGD	YLR274w.
SGD	S000004264. CDC46.
Phylogenomic databases
eggNOG	fuNOG07041.
GeneTree	EFGT00050000003095.
HOGENOM	HBG546212.
OMA	ELQHRMQ.
OrthoDB	EOG4KWP24.
Enzyme and pathway databases
Reactome	REACT_101785. DNA Replication. REACT_108233. Cell Cycle, Mitotic.
Gene expression databases
ArrayExpress	P29496.
Genevestigator	P29496.
GermOnline	YLR274W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR008048. MCM_5. 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. 2 hits.
KO	K02209.
Pfam	PF00493. MCM. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01661. MCMPROTEIN5.
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	967492.

Entry information

Entry name

MCM5_YEAST

Accession

Primary (citable) accession number: P29496
Secondary accession number(s): D6VYS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	December 14, 2011
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program