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Protein

DNA replication licensing factor MCM6

Gene

MCM6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi575 – 582ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA helicase activity Source: InterPro
  • DNA replication origin binding Source: SGD
  • single-stranded DNA-dependent ATPase activity Source: SGD

GO - Biological processi

  • DNA replication initiation Source: InterPro
  • DNA strand elongation involved in DNA replication Source: SGD
  • DNA unwinding involved in DNA replication Source: SGD
  • double-strand break repair via break-induced replication Source: SGD
  • nuclear DNA replication Source: SGD
  • pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30681-MONOMER.
ReactomeiR-SCE-176974. Unwinding of DNA.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69052. Switching of origins to a post-replicative state.
R-SCE-69300. Removal of licensing factors from origins.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM6 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance protein 6
Gene namesi
Name:MCM6
Ordered Locus Names:YGL201C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL201C.
SGDiS000003169. MCM6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • DNA replication preinitiation complex Source: SGD
  • MCM complex Source: SGD
  • MCM core complex Source: SGD
  • nuclear pre-replicative complex Source: SGD
  • nucleoplasm Source: Reactome
  • nucleus Source: SGD
  • replication fork protection complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi581K → A: Loss of MCM2-7 complex helicase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001941171 – 1017DNA replication licensing factor MCM6Add BLAST1017

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei78PhosphoserineCombined sources1
Modified residuei249PhosphoserineCombined sources1
Modified residuei372PhosphoserineCombined sources1
Modified residuei766PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53091.
PRIDEiP53091.

PTM databases

iPTMnetiP53091.

Interactioni

Subunit structurei

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 MCM10.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MCM10P323545EBI-10556,EBI-5965
MCM4P306655EBI-10556,EBI-4326

Protein-protein interaction databases

BioGridi33056. 73 interactors.
DIPiDIP-1294N.
IntActiP53091. 55 interactors.
MINTiMINT-397018.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8061-1017[»]
3JC5electron microscopy4.7061-1017[»]
3JC6electron microscopy3.7061-1017[»]
3JC7electron microscopy4.8061-1017[»]
ProteinModelPortaliP53091.
SMRiP53091.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini525 – 732MCMAdd BLAST208

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi707 – 710Arginine finger4

Sequence similaritiesi

Belongs to the MCM family.Curated
Contains 1 MCM domain.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074860.
HOGENOMiHOG000224130.
InParanoidiP53091.
KOiK02542.
OMAiGTNIRGE.
OrthoDBiEOG092C0VUM.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PANTHERiPTHR11630:SF43. PTHR11630:SF43. 5 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
PF17207. MCM_OB. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53091-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPFPADTP SSNRPSNSSP PPSSIGAGFG SSSGLDSQIG SRLHFPSSSQ
60 70 80 90 100
PHVSNSQTGP FVNDSTQFSS QRLQTDGSAT NDMEGNEPAR SFKSRALNHV
110 120 130 140 150
KKVDDVTGEK VREAFEQFLE DFSVQSTDTG EVEKVYRAQI EFMKIYDLNT
160 170 180 190 200
IYIDYQHLSM RENGALAMAI SEQYYRFLPF LQKGLRRVVR KYAPELLNTS
210 220 230 240 250
DSLKRSEGDE GQADEDEQQD DDMNGSSLPR DSGSSAAPGN GTSAMATRSI
260 270 280 290 300
TTSTSPEQTE RVFQISFFNL PTVHRIRDIR SEKIGSLLSI SGTVTRTSEV
310 320 330 340 350
RPELYKASFT CDMCRAIVDN VEQSFKYTEP TFCPNPSCEN RAFWTLNVTR
360 370 380 390 400
SRFLDWQKVR IQENANEIPT GSMPRTLDVI LRGDSVERAK PGDRCKFTGV
410 420 430 440 450
EIVVPDVTQL GLPGVKPSST LDTRGISKTT EGLNSGVTGL RSLGVRDLTY
460 470 480 490 500
KISFLACHVI SIGSNIGASS PDANSNNRET ELQMAANLQA NNVYQDNERD
510 520 530 540 550
QEVFLNSLSS DEINELKEMV KDEHIYDKLV RSIAPAVFGH EAVKKGILLQ
560 570 580 590 600
MLGGVHKSTV EGIKLRGDIN ICVVGDPSTS KSQFLKYVVG FAPRSVYTSG
610 620 630 640 650
KASSAAGLTA AVVRDEEGGD YTIEAGALML ADNGICCIDE FDKMDISDQV
660 670 680 690 700
AIHEAMEQQT ISIAKAGIHA TLNARTSILA AANPVGGRYN RKLSLRGNLN
710 720 730 740 750
MTAPIMSRFD LFFVILDDCN EKIDTELASH IVDLHMKRDE AIEPPFSAEQ
760 770 780 790 800
LRRYIKYART FKPILTKEAR SYLVEKYKEL RKDDAQGFSR SSYRITVRQL
810 820 830 840 850
ESMIRLSEAI ARANCVDEIT PSFIAEAYDL LRQSIIRVDV DDVEMDEEFD
860 870 880 890 900
NIESQSHAAS GNNDDNDDGT GSGVITSEPP ADIEEGQSEA TARPGTSEKK
910 920 930 940 950
KTTVTYDKYV SMMNMIVRKI AEVDREGAEE LTAVDIVDWY LLQKENDLGS
960 970 980 990 1000
LAEYWEERRL AFKVIKRLVK DRILMEIHGT RHNLRDLENE ENENNKTVYV
1010
IHPNCEVLDQ LEPQDSS
Length:1,017
Mass (Da):112,978
Last modified:October 5, 2010 - v2
Checksum:i03AB793134E64A50
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti179P → A in CAA96913 (PubMed:9169869).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY258324 Genomic DNA. Translation: AAO89010.1.
Z72723 Genomic DNA. Translation: CAA96913.1.
Y13624 Genomic DNA. Translation: CAA73947.1.
BK006941 Genomic DNA. Translation: DAA07914.1.
PIRiS64219.
RefSeqiNP_011314.2. NM_001181066.1.

Genome annotation databases

EnsemblFungiiYGL201C; YGL201C; YGL201C.
GeneIDi852673.
KEGGisce:YGL201C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY258324 Genomic DNA. Translation: AAO89010.1.
Z72723 Genomic DNA. Translation: CAA96913.1.
Y13624 Genomic DNA. Translation: CAA73947.1.
BK006941 Genomic DNA. Translation: DAA07914.1.
PIRiS64219.
RefSeqiNP_011314.2. NM_001181066.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8061-1017[»]
3JC5electron microscopy4.7061-1017[»]
3JC6electron microscopy3.7061-1017[»]
3JC7electron microscopy4.8061-1017[»]
ProteinModelPortaliP53091.
SMRiP53091.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33056. 73 interactors.
DIPiDIP-1294N.
IntActiP53091. 55 interactors.
MINTiMINT-397018.

PTM databases

iPTMnetiP53091.

Proteomic databases

MaxQBiP53091.
PRIDEiP53091.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL201C; YGL201C; YGL201C.
GeneIDi852673.
KEGGisce:YGL201C.

Organism-specific databases

EuPathDBiFungiDB:YGL201C.
SGDiS000003169. MCM6.

Phylogenomic databases

GeneTreeiENSGT00550000074860.
HOGENOMiHOG000224130.
InParanoidiP53091.
KOiK02542.
OMAiGTNIRGE.
OrthoDBiEOG092C0VUM.

Enzyme and pathway databases

BioCyciYEAST:G3O-30681-MONOMER.
ReactomeiR-SCE-176974. Unwinding of DNA.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69052. Switching of origins to a post-replicative state.
R-SCE-69300. Removal of licensing factors from origins.

Miscellaneous databases

PROiP53091.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PANTHERiPTHR11630:SF43. PTHR11630:SF43. 5 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
PF17207. MCM_OB. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCM6_YEAST
AccessioniPrimary (citable) accession number: P53091
Secondary accession number(s): D6VTV3, Q870M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 5, 2010
Last modified: November 30, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 13400 molecules/cell in log phase SD medium.1 Publication
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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.