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Protein

DNA replication licensing factor MCM4

Gene

dpa

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. Essential role in mitotic DNA replication but not in endoreplication.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi512 – 5198ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • DNA duplex unwinding Source: GOC
  • DNA replication Source: FlyBase
  • DNA replication initiation Source: InterPro
  • mitotic spindle organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

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 MCM4 (EC:3.6.4.12)
Alternative name(s):
Protein disc proliferation abnormal
Gene namesi
Name:dpa
ORF Names:CG1616
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0015929. dpa.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi518 – 5181K → A: Slihgtly reduces complex helicase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 866866DNA replication licensing factor MCM4PRO_0000194104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551Phosphoserine2 Publications
Modified residuei81 – 811Phosphoserine1 Publication
Modified residuei87 – 871Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ26454.

PTM databases

iPTMnetiQ26454.

Expressioni

Gene expression databases

BgeeiQ26454.
ExpressionAtlasiQ26454. differential.
GenevisibleiQ26454. 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

Binary interactionsi

WithEntry#Exp.IntActNotes
Mcm6Q9V4613EBI-175772,EBI-869161

Protein-protein interaction databases

BioGridi61555. 7 interactions.
DIPiDIP-35346N.
IntActiQ26454. 8 interactions.
STRINGi7227.FBpp0088055.

Structurei

3D structure databases

ProteinModelPortaliQ26454.
SMRiQ26454. Positions 168-776.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini460 – 669210MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi644 – 6474Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0478. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00790000123057.
InParanoidiQ26454.
KOiK02212.
OMAiKNTIRIC.
OrthoDBiEOG78D7JF.
PhylomeDBiQ26454.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008047. MCM_4.
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.
PR01660. MCMPROTEIN4.
SMARTiSM00382. AAA. 1 hit.
SM00350. 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.

Q26454-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPARSPSV GGATPKQGAR TPTRGIASQD VETPMRMGPG RAVRPSDNIS
60 70 80 90 100
LPPTSPGNIS LPATSPARGL GANMSEIDLS SPLNYGTPSS MGSIRTPRSG
110 120 130 140 150
IRGTPLRARP DIRTDKRIRQ VAIGGGSGLE PIPEKGSETT DPVSESSQAP
160 170 180 190 200
QLVVWGTNVV VSQCKSKFKS FIMRFIDPSA EQDEISENID VNQPLYLQKL
210 220 230 240 250
EEIHTLEEPY LNLNCAHLKT FDQDLYRQLI CYPQEVIPGF DMAINEMFFE
260 270 280 290 300
RYPAALLEHQ IQVRPFNADK TRNMRSLNPE DMDQLISISG MVIRSSNVIP
310 320 330 340 350
EMREAFFSCN ICSFSTTVEV DRGRINQPTL CTNCNTNHCF RLIHNRSEFT
360 370 380 390 400
DKQLVKLQES PDDMAAGQTP HNVLLYAHND LVDKVQPGDR VTVTGIYRAT
410 420 430 440 450
PLKTGGLSSS VKSVYKTHVD VVHFRKVDNK RLYEDEEGKD HIFPPERVEL
460 470 480 490 500
LQLLAKKPDI YDRLARAIAP SIYENDDIKK GILLQLFGGT KKKHATLGRQ
510 520 530 540 550
NFRSEIHLLL CGDPGTSKSQ MLQYVFNLVP RSQYTSGRGS SAVGLTAYVT
560 570 580 590 600
KDPETRQLVL QTGALVLADN GVCCIDEFDK MNDSTRSVLH EVMEQQTLSI
610 620 630 640 650
AKAGIICQLN ARTSILAAAN PAESQWNKRK NIIDNVQLPH TLLSRFDLIF
660 670 680 690 700
LVLDPQDEIF DKRLASHLVS LYYVTRHEEE DTMFDMSVLR DYIAYAREHL
710 720 730 740 750
SPTLSDEAQQ RLIQAYVDMR KVGAGRGQIS AYPRQLESLI RLSEAHAKVR
760 770 780 790 800
LSNQVELLDV EEAWRLHREA LKQSATDPLS GKIDVGILTT GLSTAARKKR
810 820 830 840 850
ADLVAAIKEN LKKKGKVLTV PYQKLFSDIK EGSQIMITRE QFEDALKEVQ
860
DEGAIVVMGK NTIRIC
Length:866
Mass (Da):96,610
Last modified:November 2, 2001 - v2
Checksum:iCF6ED69D2ADDA04E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti435 – 4351D → E in AAB35644 (PubMed:7489728).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S80255 mRNA. Translation: AAB35644.1.
AE013599 Genomic DNA. Translation: AAF59242.1.
PIRiS59872.
RefSeqiNP_001286160.1. NM_001299231.1.
NP_477185.1. NM_057837.5.
UniGeneiDm.21562.

Genome annotation databases

EnsemblMetazoaiFBtr0088982; FBpp0088055; FBgn0015929.
FBtr0345797; FBpp0311783; FBgn0015929.
GeneIDi35679.
KEGGidme:Dmel_CG1616.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S80255 mRNA. Translation: AAB35644.1.
AE013599 Genomic DNA. Translation: AAF59242.1.
PIRiS59872.
RefSeqiNP_001286160.1. NM_001299231.1.
NP_477185.1. NM_057837.5.
UniGeneiDm.21562.

3D structure databases

ProteinModelPortaliQ26454.
SMRiQ26454. Positions 168-776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61555. 7 interactions.
DIPiDIP-35346N.
IntActiQ26454. 8 interactions.
STRINGi7227.FBpp0088055.

PTM databases

iPTMnetiQ26454.

Proteomic databases

PaxDbiQ26454.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088982; FBpp0088055; FBgn0015929.
FBtr0345797; FBpp0311783; FBgn0015929.
GeneIDi35679.
KEGGidme:Dmel_CG1616.

Organism-specific databases

CTDi103997.
FlyBaseiFBgn0015929. dpa.

Phylogenomic databases

eggNOGiKOG0478. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00790000123057.
InParanoidiQ26454.
KOiK02212.
OMAiKNTIRIC.
OrthoDBiEOG78D7JF.
PhylomeDBiQ26454.

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

GenomeRNAii35679.
NextBioi794682.
PROiQ26454.

Gene expression databases

BgeeiQ26454.
ExpressionAtlasiQ26454. differential.
GenevisibleiQ26454. DM.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008047. MCM_4.
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.
PR01660. MCMPROTEIN4.
SMARTiSM00382. AAA. 1 hit.
SM00350. 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. "dpa, a member of the MCM family, is required for mitotic DNA replication but not endoreplication in Drosophila."
    Feger G., Vaessin H., Su T.T., Wolff E., Jan L.Y., Jan Y.N.
    EMBO J. 14:5387-5398(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "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.
  5. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-81 AND THR-87, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  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-518.

Entry informationi

Entry nameiMCM4_DROME
AccessioniPrimary (citable) accession number: Q26454
Secondary accession number(s): Q9V4M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 2, 2001
Last modified: May 11, 2016
This is version 132 of the entry and version 2 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.