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Protein

DNA replication licensing factor Mcm6

Gene

Mcm6

Organism
Drosophila melanogaster (Fruit fly)
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 Required for DNA replication and cell proliferation. Required for mitotic cycles, endocycles, and the special S phase associated with the amplification of chorion genes; has a role in origin unwinding or fork elongation at chorion loci.3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri152 – 17928C4-typeSequence analysisAdd
BLAST
Nucleotide bindingi388 – 3958ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • DNA duplex unwinding Source: GOC
  • DNA replication Source: UniProtKB
  • DNA replication initiation Source: InterPro
  • eggshell chorion gene amplification Source: FlyBase
  • lateral inhibition Source: FlyBase
  • mitotic nuclear division Source: UniProtKB-KW
  • oogenesis Source: FlyBase
  • pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, DNA replication, Mitosis

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-176187. Activation of ATR in response to replication stress.
R-DME-68867. Assembly of the pre-replicative complex.
R-DME-68949. Orc1 removal from chromatin.
R-DME-68962. Activation of the pre-replicative complex.
R-DME-69052. Switching of origins to a post-replicative state.
R-DME-69300. Removal of licensing factors from origins.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor Mcm6 (EC:3.6.4.12)
Short name:
DmMCM6
Gene namesi
Name:Mcm6Imported
ORF Names:CG4039
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0025815. Mcm6.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Associated with chromatin during cell cycles.

GO - Cellular componenti

  • MCM complex Source: InterPro
  • nuclear pre-replicative complex Source: FlyBase
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi157 – 1571T → M in allele 4; homozygous lethal. 1 Publication
Mutagenesisi388 – 3881G → D in allele 5; homozygous lethal. 1 Publication
Mutagenesisi394 – 3941K → A: Slihgtly reduces complex helicase activity. 1 Publication
Mutagenesisi676 – 6761M → K in allele K1214; eggs exhibit thin shell and flimsy dorsal appendages. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 817817DNA replication licensing factor Mcm6PRO_0000233315Add
BLAST

Proteomic databases

PaxDbiQ9V461.
PRIDEiQ9V461.

Expressioni

Tissue specificityi

In stage 12 embryos, strongly expressed in the CNS and weakly in the gut.1 Publication

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiQ9V461.
ExpressionAtlasiQ9V461. differential.
GenevisibleiQ9V461. DM.

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 (Probable). The heterodimers of Mcm4/Mcm6 and Mcm3/Mcm5 interact with Mcm2 and Mcm7.Curated1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
dpaQ264543EBI-869161,EBI-175772
Mcm2P497355EBI-869161,EBI-138228

Protein-protein interaction databases

BioGridi58089. 7 interactions.
DIPiDIP-35347N.
IntActiQ9V461. 5 interactions.
STRINGi7227.FBpp0070913.

Structurei

3D structure databases

ProteinModelPortaliQ9V461.
SMRiQ9V461. Positions 13-652, 701-817.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini338 – 544207MCMSequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi520 – 5234Arginine finger

Sequence similaritiesi

Belongs to the MCM family.Sequence analysis
Contains 1 MCM domain.Sequence analysis

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri152 – 17928C4-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0480. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00550000074860.
InParanoidiQ9V461.
KOiK02542.
OMAiIDMENNG.
OrthoDBiEOG7CCBQC.
PhylomeDBiQ9V461.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9V461-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVADAQVGQ LRVKDEVGIR AQKLFQDFLE EFKEDGEIKY TRPAASLESP
60 70 80 90 100
DRCTLEVSFE DVEKYDQNLA TAIIEEYYHI YPFLCQSVSN YVKDRIGLKT
110 120 130 140 150
QKDCYVAFTE VPTRHKVRDL TTSKIGTLIR ISGQVVRTHP VHPELVSGVF
160 170 180 190 200
MCLDCQTEIR NVEQQFKFTN PTICRNPVCS NRKRFMLDVE KSLFLDFQKI
210 220 230 240 250
RIQETQAELP RGCIPRAVEI ILRSELVETV QAGDRYDFTG TLIVVPDVSV
260 270 280 290 300
LAGVGTRAEN SSRHKPGEGM DGVTGLKALG MRELNYRMAF LACSVQATTA
310 320 330 340 350
RFGGTDLPMS EVTAEDMKKQ MTDAEWHKIY EMSKDRNLYQ NLISSLFPSI
360 370 380 390 400
YGNDEVKRGI LLQQFGGVAK TTTEKTSLRG DINVCIVGDP STAKSQFLKQ
410 420 430 440 450
VSDFSPRAIY TSGKASSAAG LTAAVVRDEE SFDFVIEAGA LMLADNGICC
460 470 480 490 500
IDEFDKMDQR DQVAIHEAME QQTISIARAG VRATLNARTS ILAAANPING
510 520 530 540 550
RYDRSKSLQQ NIQLSAPIMS RFDLFFILVD ECNEVVDYAI ARKIVDLHSN
560 570 580 590 600
IEESVERAYT REEVLRYVTF ARQFKPVISQ EAGHMLVENY GHLRQRDTGT
610 620 630 640 650
SGRSTWRITV RQLESMIRLS EAMAKLECSN RVLERHVKEA FRLLNKSIIR
660 670 680 690 700
VEQPDIHLDD DEGLDMDDGI QHDIDMENNG AAANVDENNG MDTSASGAVQ
710 720 730 740 750
KKKFTLSFED YKNLSTMLVL HMRAEEARCE VEGNDTGIKR SNVVTWYLEQ
760 770 780 790 800
VADQIESEDE LISRKNLIEK LIDRLIYHDQ VIIPLKTSTL KPRIQVQKDF
810
VEEDDPLLVV HPNYVVE
Length:817
Mass (Da):92,353
Last modified:May 1, 2000 - v1
Checksum:i0B7921FB3D888980
GO

Sequence cautioni

The sequence AAK93526.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 112QL → HV in BAA34732 (PubMed:9795205).Curated
Sequence conflicti550 – 5501N → K in BAA34732 (PubMed:9795205).Curated
Sequence conflicti695 – 6951A → G (PubMed:9795205).Curated
Sequence conflicti695 – 6951A → G (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010108 mRNA. Translation: BAA34732.1.
AF124744 mRNA. Translation: AAD32858.1.
AE014298 Genomic DNA. Translation: AAF46184.1.
AY052102 mRNA. Translation: AAK93526.1. Different initiation.
RefSeqiNP_511065.1. NM_078510.3.
UniGeneiDm.2944.

Genome annotation databases

EnsemblMetazoaiFBtr0070952; FBpp0070913; FBgn0025815.
GeneIDi31603.
KEGGidme:Dmel_CG4039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010108 mRNA. Translation: BAA34732.1.
AF124744 mRNA. Translation: AAD32858.1.
AE014298 Genomic DNA. Translation: AAF46184.1.
AY052102 mRNA. Translation: AAK93526.1. Different initiation.
RefSeqiNP_511065.1. NM_078510.3.
UniGeneiDm.2944.

3D structure databases

ProteinModelPortaliQ9V461.
SMRiQ9V461. Positions 13-652, 701-817.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58089. 7 interactions.
DIPiDIP-35347N.
IntActiQ9V461. 5 interactions.
STRINGi7227.FBpp0070913.

Proteomic databases

PaxDbiQ9V461.
PRIDEiQ9V461.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070952; FBpp0070913; FBgn0025815.
GeneIDi31603.
KEGGidme:Dmel_CG4039.

Organism-specific databases

CTDi4175.
FlyBaseiFBgn0025815. Mcm6.

Phylogenomic databases

eggNOGiKOG0480. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00550000074860.
InParanoidiQ9V461.
KOiK02542.
OMAiIDMENNG.
OrthoDBiEOG7CCBQC.
PhylomeDBiQ9V461.

Enzyme and pathway databases

ReactomeiR-DME-176187. Activation of ATR in response to replication stress.
R-DME-68867. Assembly of the pre-replicative complex.
R-DME-68949. Orc1 removal from chromatin.
R-DME-68962. Activation of the pre-replicative complex.
R-DME-69052. Switching of origins to a post-replicative state.
R-DME-69300. Removal of licensing factors from origins.

Miscellaneous databases

GenomeRNAii31603.
NextBioi774413.
PROiQ9V461.

Gene expression databases

BgeeiQ9V461.
ExpressionAtlasiQ9V461. differential.
GenevisibleiQ9V461. DM.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression during development of Drosophila melanogaster MCM3, MCM6 and MCM7."
    Ohno K., Hirose F., Inoue Y.H., Takisawa H., Mimura S., Hashimoto Y., Kiyono T., Nishida Y., Matsukage A.
    Gene 217:177-185(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Tissue: Oocyte1 Publication.
  2. "Identification and complete cDNA sequence of the missing Drosophila MCMs: DmMCM3, DmMCM6 and DmMCM7."
    Feger G.
    Gene 227:149-155(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Drosophila minichromosome maintenance 6 is required for chorion gene amplification and genomic replication."
    Schwed G., May N., Pechersky Y., Calvi B.R.
    Mol. Biol. Cell 13:607-620(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MCM2; MCM4 AND MCM5, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-157; GLY-388 AND MET-676.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 231-817.
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  7. "Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase."
    Moyer S.E., Lewis P.W., Botchan M.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:10236-10241(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX.
  8. "Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins."
    Ilves I., Petojevic T., Pesavento J.J., Botchan M.R.
    Mol. Cell 37:247-258(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, MUTAGENESIS OF LYS-394.

Entry informationi

Entry nameiMCM6_DROME
AccessioniPrimary (citable) accession number: Q9V461
Secondary accession number(s): O96047, Q960E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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.