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Protein

DNA replication licensing factor Mcm3

Gene

Mcm3

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) (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 bindingi340 – 3478ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • DNA duplex unwinding Source: GOC
  • DNA replication initiation Source: InterPro
  • mitotic G2 DNA damage checkpoint Source: FlyBase
  • neurogenesis 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 Mcm3 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance 3 protein
Short name:
DmMCM3
Gene namesi
Name:Mcm3
Synonyms:Mcm3-RA
ORF Names:CG4206
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0024332. Mcm3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi346 – 3461K → A: Greatly reduces complex helicase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 819819DNA replication licensing factor Mcm3PRO_0000406421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei522 – 5221Phosphoserine1 Publication
Modified residuei538 – 5381Phosphotyrosine1 Publication
Modified residuei664 – 6641Phosphoserine1 Publication
Modified residuei666 – 6661Phosphoserine1 Publication
Modified residuei680 – 6801Phosphoserine1 Publication
Modified residuei682 – 6821Phosphoserine1 Publication
Modified residuei690 – 6901Phosphothreonine1 Publication
Modified residuei692 – 6921Phosphothreonine1 Publication
Modified residuei697 – 6971Phosphoserine2 Publications
Modified residuei735 – 7351Phosphoserine1 Publication
Modified residuei739 – 7391Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9XYU1.
PRIDEiQ9XYU1.

PTM databases

iPTMnetiQ9XYU1.

Expressioni

Gene expression databases

BgeeiQ9XYU1.
GenevisibleiQ9XYU1. 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
Mcm5Q9VGW63EBI-103930,EBI-83298

Protein-protein interaction databases

BioGridi57959. 5 interactions.
IntActiQ9XYU1. 4 interactions.
MINTiMINT-990984.
STRINGi7227.FBpp0070729.

Structurei

3D structure databases

ProteinModelPortaliQ9XYU1.
SMRiQ9XYU1. Positions 43-646.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini290 – 496207MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi472 – 4754Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0479. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00550000075022.
InParanoidiQ9XYU1.
KOiK02541.
OMAiLGSMVCV.
OrthoDBiEOG7V1FQ3.
PhylomeDBiQ9XYU1.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008046. Mcm3.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01659. MCMPROTEIN3.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9XYU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHEGEQFIK DIQREYVDFL DDEEDQGIYA GHVKDMIAEK SKRLIVNVND
60 70 80 90 100
LKRKNPQRAL GLLSNAADEQ LAFGRALKEY ASTVDPGYAK MHEDLFVGFE
110 120 130 140 150
GCFGNRHVTP RSLTSIYLGN MVCVEGIVTK VSLIRPKVVR SVHYCPNTRK
160 170 180 190 200
VMERKYTDLT SFEAVPSGAA YPTKDEDGNL LETEYGLSVY KDHQTLTIQE
210 220 230 240 250
MPEKAPAGQL PRSVDIVCDD DLVDRCKPGD RVQIVGSYRC LPGKRGGYTS
260 270 280 290 300
GTFRTVLLAN NISLLSKESN LDISREDIML CKKLAKNNDI FELLSKSLAP
310 320 330 340 350
SIHGHAYVKQ AILCLLLGGV EKILPNGTRL RGDINVLLIG DPSVAKSQLL
360 370 380 390 400
RYVLNTAPRA IPTTGRGSSG VGLTAAVTTD QETGERRLEA GAMVLADRGV
410 420 430 440 450
VCIDEFDKMS DIDRTAIHEV MEQGRVTISK AGIHASLNAR CSVLAAANPV
460 470 480 490 500
YGRYDQYKTP MENIGLQDSL LSRFDLLFVM LDVIDSDVDQ MISDHVVRMH
510 520 530 540 550
RYRNPKEADG EPLSMGSSYA DSLSFVSSSE EKKDTEVYEK YDALLHGKSR
560 570 580 590 600
QRHEKILSVE FMRKYIHIAK CMKPKLGEQA CEAIANEYSR LRSQEAVETD
610 620 630 640 650
VARTQPITAR TLETLIRLST AHARARMSKS VTIDDAHAAI ELVQFAYFKK
660 670 680 690 700
VLDKDRPSKR RRNSGSDAED DNGEASSQRS PSRRSKRTRT ATVGADSDEE
710 720 730 740 750
DIEPPQPDAG DLTRRETRRS LPARSVAMLM ASPSSEEQSV ATSTTEPAII
760 770 780 790 800
SDARLGEFKN NLQRLFREAR EQSLALARIT TAINVGSQEP FTAGEIEAAV
810
HRMTEDNQIM VADDIVFLI
Length:819
Mass (Da):90,918
Last modified:November 1, 1999 - v1
Checksum:iCE4C14FE89BA8113
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411S → C in BAA34731 (PubMed:9795205).Curated
Sequence conflicti193 – 1931H → D in BAA34731 (PubMed:9795205).Curated
Sequence conflicti264 – 2641L → Q in BAA34731 (PubMed:9795205).Curated
Sequence conflicti551 – 5511Q → L in BAA34731 (PubMed:9795205).Curated
Sequence conflicti597 – 5971V → D in BAA34731 (PubMed:9795205).Curated
Sequence conflicti720 – 7201S → L in BAA34731 (PubMed:9795205).Curated
Sequence conflicti795 – 7962EI → AL in BAA34731 (PubMed:9795205).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010107 mRNA. Translation: BAA34731.1.
AF124745 mRNA. Translation: AAD32859.1.
AE014298 Genomic DNA. Translation: AAF46023.1.
BT046156 mRNA. Translation: ACI46544.1.
RefSeqiNP_511048.2. NM_078493.4.
UniGeneiDm.2020.

Genome annotation databases

EnsemblMetazoaiFBtr0070762; FBpp0070729; FBgn0024332.
GeneIDi31449.
KEGGidme:Dmel_CG4206.
UCSCiCG4206-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010107 mRNA. Translation: BAA34731.1.
AF124745 mRNA. Translation: AAD32859.1.
AE014298 Genomic DNA. Translation: AAF46023.1.
BT046156 mRNA. Translation: ACI46544.1.
RefSeqiNP_511048.2. NM_078493.4.
UniGeneiDm.2020.

3D structure databases

ProteinModelPortaliQ9XYU1.
SMRiQ9XYU1. Positions 43-646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57959. 5 interactions.
IntActiQ9XYU1. 4 interactions.
MINTiMINT-990984.
STRINGi7227.FBpp0070729.

PTM databases

iPTMnetiQ9XYU1.

Proteomic databases

PaxDbiQ9XYU1.
PRIDEiQ9XYU1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070762; FBpp0070729; FBgn0024332.
GeneIDi31449.
KEGGidme:Dmel_CG4206.
UCSCiCG4206-RA. d. melanogaster.

Organism-specific databases

CTDi4172.
FlyBaseiFBgn0024332. Mcm3.

Phylogenomic databases

eggNOGiKOG0479. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00550000075022.
InParanoidiQ9XYU1.
KOiK02541.
OMAiLGSMVCV.
OrthoDBiEOG7V1FQ3.
PhylomeDBiQ9XYU1.

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

GenomeRNAii31449.
PROiQ9XYU1.

Gene expression databases

BgeeiQ9XYU1.
GenevisibleiQ9XYU1. DM.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008046. Mcm3.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01659. MCMPROTEIN3.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
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. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    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. "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-697; SER-735 AND SER-739, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "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-522; TYR-538; SER-664; SER-666; SER-680; SER-682; THR-690; THR-692 AND SER-697, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  9. "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-346.

Entry informationi

Entry nameiMCM3_DROME
AccessioniPrimary (citable) accession number: Q9XYU1
Secondary accession number(s): P91675
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 136 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.