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Protein

DNA replication licensing factor Mcm7

Gene

Mcm7

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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi381 – 3888ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • DNA duplex unwinding Source: GOC
  • DNA replication initiation Source: InterPro
  • mitotic G2 DNA damage checkpoint 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, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

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 Mcm7 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance 7 protein
Short name:
DmMCM3
Gene namesi
Name:Mcm7
ORF Names:CG4978
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0020633. Mcm7.

Subcellular locationi

GO - Cellular componenti

  • MCM complex Source: InterPro
  • microtubule associated complex Source: FlyBase
  • nuclear pre-replicative complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi387 – 3871K → A: Reduces complex helicase activity. 1 Publication
Mutagenesisi514 – 5141R → A: Reduces complex helicase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720DNA replication licensing factor Mcm7PRO_0000406423Add
BLAST

Proteomic databases

PaxDbiQ9XYU0.
PRIDEiQ9XYU0.

Expressioni

Gene expression databases

BgeeiQ9XYU0.
ExpressionAtlasiQ9XYU0. differential.
GenevisibleiQ9XYU0. 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).Curated1 Publication

Protein-protein interaction databases

BioGridi64419. 9 interactions.
DIPiDIP-59081N.
IntActiQ9XYU0. 1 interaction.
STRINGi7227.FBpp0076312.

Structurei

3D structure databases

ProteinModelPortaliQ9XYU0.
SMRiQ9XYU0. Positions 5-646.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini332 – 538207MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi513 – 5164Arginine finger

Sequence similaritiesi

Contains 1 MCM domain.Curated

Phylogenomic databases

eggNOGiKOG0482. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00670000098113.
InParanoidiQ9XYU0.
KOiK02210.
OMAiQTRACRF.
OrthoDBiEOG7N0C42.
PhylomeDBiQ9XYU0.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008050. MCM7.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF26. PTHR11630:SF26. 2 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 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.

Q9XYU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARRDYAQDR ESIKTFLSEF CKCDDDGKKE FVYGSQLVKL AHREQVLITI
60 70 80 90 100
DLDDLAEFNE SLAEAVVDNC RRYTSIFSDV IAELLPSYKQ QEVHAKDALD
110 120 130 140 150
VYIEHRLMME SRTRNPMEQR DERNSFPSEL MKRFEVGFKP LSTEKAHSIR
160 170 180 190 200
EVKAQHIGKL VTVRGIVTRC TEVKPMMVVA TYTCDRCGSE TYQPVNSLSF
210 220 230 240 250
TPVHDCPSDD CRVNKAGGRL YLQTRGSKFV KFQEVKMQEH SDQVPVGHIP
260 270 280 290 300
RSMTIMCRGE VTRMAQPGDH IVVSGVFLPL MRTGFAQMIQ GLLSETFLQA
310 320 330 340 350
HRIICINKND EISDKDAELT PEELEELAQD DFYERLATSL APEIYGHLDV
360 370 380 390 400
KKALLLLLVG GVDKRPDGMK IRGNINICLM GDPGVAKSQL LGYISRLAVR
410 420 430 440 450
SQYTTGRGSS GVGLTAAVMK DPLTGEMTLE GGALVLADQG VCCIDEFDKM
460 470 480 490 500
ADQDRTAIHE VMEQQTISIA KAGIMTTLNA RVSILAAANP AFGRYNPRRT
510 520 530 540 550
VEQNIQLPAA LLSRFDLLWL IQDKPDRDND LRLAKHITYV HSHSKQPPTR
560 570 580 590 600
VKALDMNLMR RYINLCKRKN PTIPDELTDY IVGAYVELRR EARNQKDMTF
610 620 630 640 650
TSARNLLGIL RLSTALARLR LSDSVEKDDV AEALRLLEMS KDSLNQIHEH
660 670 680 690 700
QKGHVPNTSD RIFAIVRELA GSGKAVKISD IMDRCTTKGF KPDQVDKCID
710 720
DYEELNVWQV NMGRTKITFM
Length:720
Mass (Da):81,284
Last modified:November 1, 1999 - v1
Checksum:i09286B4D5E406756
GO

Sequence cautioni

The sequence BAA34733.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti506 – 5061Q → E in BAA34733 (PubMed:9795205).Curated
Sequence conflicti618 – 6181R → W in BAA34733 (PubMed:9795205).Curated
Sequence conflicti624 – 6241S → T in BAA34733 (PubMed:9795205).Curated
Sequence conflicti659 – 6591S → T in BAA34733 (PubMed:9795205).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010109 mRNA. Translation: BAA34733.1. Sequence problems.
AF124743 mRNA. Translation: AAD32857.1.
AE014296 Genomic DNA. Translation: AAF50357.1.
BT001526 mRNA. Translation: AAN71281.1.
RefSeqiNP_523984.1. NM_079260.3.
UniGeneiDm.7221.

Genome annotation databases

EnsemblMetazoaiFBtr0076585; FBpp0076312; FBgn0020633.
GeneIDi39014.
KEGGidme:Dmel_CG4978.
UCSCiCG4978-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010109 mRNA. Translation: BAA34733.1. Sequence problems.
AF124743 mRNA. Translation: AAD32857.1.
AE014296 Genomic DNA. Translation: AAF50357.1.
BT001526 mRNA. Translation: AAN71281.1.
RefSeqiNP_523984.1. NM_079260.3.
UniGeneiDm.7221.

3D structure databases

ProteinModelPortaliQ9XYU0.
SMRiQ9XYU0. Positions 5-646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64419. 9 interactions.
DIPiDIP-59081N.
IntActiQ9XYU0. 1 interaction.
STRINGi7227.FBpp0076312.

Proteomic databases

PaxDbiQ9XYU0.
PRIDEiQ9XYU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076585; FBpp0076312; FBgn0020633.
GeneIDi39014.
KEGGidme:Dmel_CG4978.
UCSCiCG4978-RA. d. melanogaster.

Organism-specific databases

CTDi4176.
FlyBaseiFBgn0020633. Mcm7.

Phylogenomic databases

eggNOGiKOG0482. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00670000098113.
InParanoidiQ9XYU0.
KOiK02210.
OMAiQTRACRF.
OrthoDBiEOG7N0C42.
PhylomeDBiQ9XYU0.

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

GenomeRNAii39014.
PROiQ9XYU0.

Gene expression databases

BgeeiQ9XYU0.
ExpressionAtlasiQ9XYU0. differential.
GenevisibleiQ9XYU0. DM.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008050. MCM7.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF26. PTHR11630:SF26. 2 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 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...

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].
  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].
  3. "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: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  6. "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.
  7. "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-387 AND ARG-514.

Entry informationi

Entry nameiMCM7_DROME
AccessioniPrimary (citable) accession number: Q9XYU0
Secondary accession number(s): P91674
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 131 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.