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Protein

DNA replication licensing factor MCM7

Gene

MCM7

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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi460 – 467ATPSequence analysis8

GO - Molecular functioni

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

GO - Biological processi

  • chromatin silencing at silent mating-type cassette Source: SGD
  • chromatin silencing at telomere Source: SGD
  • DNA replication initiation Source: SGD
  • 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-29143-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 MCM7 (EC:3.6.4.12)
Alternative name(s):
Cell division control protein 47
Minichromosome maintenance protein 7
Gene namesi
Name:MCM7
Synonyms:CDC47
Ordered Locus Names:YBR202W
ORF Names:YBR1441
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR202W.
SGDiS000000406. MCM7.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • 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

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi466K → A: Loss of MCM2-7 complex helicase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001941241 – 845DNA replication licensing factor MCM7Add BLAST845

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei811PhosphothreonineCombined sources1
Modified residuei819PhosphoserineCombined sources1
Modified residuei838PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38132.
PRIDEiP38132.

PTM databases

iPTMnetiP38132.

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 CSM1 and MCM10.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSM1P256513EBI-4300,EBI-22001
ERG26P531992EBI-4300,EBI-6514
MCM4P306653EBI-4300,EBI-4326

Protein-protein interaction databases

BioGridi32899. 43 interactors.
DIPiDIP-2408N.
IntActiP38132. 11 interactors.
MINTiMINT-637194.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8071-845[»]
3JC5electron microscopy4.7071-845[»]
3JC6electron microscopy3.7071-845[»]
3JC7electron microscopy4.8071-845[»]
ProteinModelPortaliP38132.
SMRiP38132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini410 – 617MCMAdd BLAST208

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi592 – 595Arginine finger4

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00860000134967.
InParanoidiP38132.
KOiK02210.
OMAiTCDRCGC.
OrthoDBiEOG092C0VUM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008050. MCM7.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF26. PTHR11630:SF26. 3 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
PF17207. MCM_OB. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01663. MCMPROTEIN7.
SMARTiSM00382. AAA. 1 hit.
SM00350. 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.

P38132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAALPSIQL PVDYNNLFNE ITDFLVTFKQ DTLSSDATRN ENEDENLDAE
60 70 80 90 100
NIEQHLLEKG PKYMAMLQKV ANRELNSVII DLDDILQYQN EKFLQGTQAD
110 120 130 140 150
DLVSAIQQNA NHFTELFCRA IDNNMPLPTK EIDYKDDVLD VILNQRRLRN
160 170 180 190 200
ERMLSDRTNE IRSENLMDTT MDPPSSMNDA LREVVEDETE LFPPNLTRRY
210 220 230 240 250
FLYFKPLSQN CARRYRKKAI SSKPLSVRQI KGDFLGQLIT VRGIITRVSD
260 270 280 290 300
VKPAVEVIAY TCDQCGYEVF QEVNSRTFTP LSECTSEECS QNQTKGQLFM
310 320 330 340 350
STRASKFSAF QECKIQELSQ QVPVGHIPRS LNIHVNGTLV RSLSPGDIVD
360 370 380 390 400
VTGIFLPAPY TGFKALKAGL LTETYLEAQF VRQHKKKFAS FSLTSDVEER
410 420 430 440 450
VMELITSGDV YNRLAKSIAP EIYGNLDVKK ALLLLLVGGV DKRVGDGMKI
460 470 480 490 500
RGDINVCLMG DPGVAKSQLL KAICKISPRG VYTTGKGSSG VGLTAAVMKD
510 520 530 540 550
PVTDEMILEG GALVLADNGI CCIDEFDKMD ESDRTAIHEV MEQQTISISK
560 570 580 590 600
AGINTTLNAR TSILAAANPL YGRYNPRLSP LDNINLPAAL LSRFDILFLM
610 620 630 640 650
LDIPSRDDDE KLAEHVTYVH MHNKQPDLDF TPVEPSKMRE YIAYAKTKRP
660 670 680 690 700
VMSEAVNDYV VQAYIRLRQD SKREMDSKFS FGQATPRTLL GIIRLSQALA
710 720 730 740 750
KLRLADMVDI DDVEEALRLV RVSKESLYQE TNKSKEDESP TTKIFTIIKK
760 770 780 790 800
MLQETGKNTL SYENIVKTVR LRGFTMLQLS NCIQEYSYLN VWHLINEGNT
810 820 830 840
LKFVDDGTMD TDQEDSLVST PKLAPQTTAS ANVSAQDSDI DLQDA
Length:845
Mass (Da):94,943
Last modified:July 27, 2011 - v4
Checksum:iADA66C719D96DB4A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti552G → V in CAA79689 (PubMed:8368014).Curated1
Sequence conflicti552G → V in CAA85166 (PubMed:7813418).Curated1
Sequence conflicti556 – 558TLN → NPG in CAA79689 (PubMed:8368014).Curated3
Sequence conflicti556 – 558TLN → NPG in CAA85166 (PubMed:7813418).Curated3
Sequence conflicti574Y → I in CAA79689 (PubMed:8368014).Curated1
Sequence conflicti574Y → I in CAA85166 (PubMed:7813418).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14730 Genomic DNA. Translation: AAA86309.1.
Z21487 Genomic DNA. Translation: CAA79689.1.
Z36071 Genomic DNA. Translation: CAA85166.1.
BK006936 Genomic DNA. Translation: DAA07320.2.
PIRiS34027.
RefSeqiNP_009761.4. NM_001178550.4.

Genome annotation databases

EnsemblFungiiYBR202W; YBR202W; YBR202W.
GeneIDi852501.
KEGGisce:YBR202W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14730 Genomic DNA. Translation: AAA86309.1.
Z21487 Genomic DNA. Translation: CAA79689.1.
Z36071 Genomic DNA. Translation: CAA85166.1.
BK006936 Genomic DNA. Translation: DAA07320.2.
PIRiS34027.
RefSeqiNP_009761.4. NM_001178550.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JA8electron microscopy3.8071-845[»]
3JC5electron microscopy4.7071-845[»]
3JC6electron microscopy3.7071-845[»]
3JC7electron microscopy4.8071-845[»]
ProteinModelPortaliP38132.
SMRiP38132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32899. 43 interactors.
DIPiDIP-2408N.
IntActiP38132. 11 interactors.
MINTiMINT-637194.

PTM databases

iPTMnetiP38132.

Proteomic databases

MaxQBiP38132.
PRIDEiP38132.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR202W; YBR202W; YBR202W.
GeneIDi852501.
KEGGisce:YBR202W.

Organism-specific databases

EuPathDBiFungiDB:YBR202W.
SGDiS000000406. MCM7.

Phylogenomic databases

GeneTreeiENSGT00860000134967.
InParanoidiP38132.
KOiK02210.
OMAiTCDRCGC.
OrthoDBiEOG092C0VUM.

Enzyme and pathway databases

BioCyciYEAST:G3O-29143-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

PROiP38132.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008050. MCM7.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF26. PTHR11630:SF26. 3 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
PF17207. MCM_OB. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01663. MCMPROTEIN7.
SMARTiSM00382. AAA. 1 hit.
SM00350. 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 nameiMCM7_YEAST
AccessioniPrimary (citable) accession number: P38132
Secondary accession number(s): D6VQK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 165 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 166 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.