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P49735 (MCM2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA replication licensing factor Mcm2

EC=3.6.4.12
Alternative name(s):
Minichromosome maintenance 2 protein
Short name=DmMCM2
Gene names
Name:Mcm2
ORF Names:CG7538
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7 Ref.10

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Component of the Mcm2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order Mcm2-Mcm6-Mcm4-Mcm7-Mcm3-Mcm5 (By simililarity). Interacts with Mcm10. Ref.5 Ref.6

Subcellular location

Nucleus Probable.

Sequence similarities

Belongs to the MCM family.

Contains 1 MCM domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 887887DNA replication licensing factor Mcm2
PRO_0000194090

Regions

Domain458 – 665208MCM
Zinc finger314 – 34027C4-type Potential
Nucleotide binding508 – 5158ATP Potential
Motif640 – 6434Arginine finger

Amino acid modifications

Modified residue261Phosphothreonine Ref.8
Modified residue271Phosphoserine Ref.8
Modified residue891Phosphoserine Ref.9
Modified residue921Phosphoserine Ref.9
Modified residue1241Phosphoserine Ref.8

Experimental info

Mutagenesis5141K → A: Reduces complex helicase activity. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P49735 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 26A7092109F09CBE

FASTA887100,415
        10         20         30         40         50         60 
MDNPSSPPPN TPSDAAERRD LRAAMTSPVG DFEPFENEDE ILGDQTVRDE AEEEDGEELF 

        70         80         90        100        110        120 
GDNMENDYRP MPELDHYDPA LLDDEDDFSE MSQGDRFAAE SEMRRRDRAA GIHRDDRDLG 

       130        140        150        160        170        180 
FGQSDDEDDV GPRAKRRAGE KAAVGEVEDT EMVESIENLE DTKGHSTKEW VSMLGPRTEI 

       190        200        210        220        230        240 
ANRFQSFLRT FVDERGAYTY RDRIRRMCEQ NMSSFVVSYT DLANKEHVLA YFLPEAPFQM 

       250        260        270        280        290        300 
LEIFDKVAKD MVLSIFPTYE RVTTEIHVRI SELPLIEELR TFRKLHLNQL VRTLGVVTAT 

       310        320        330        340        350        360 
TGVLPQLSVI KYDCVKCGYV LGPFVQSQNT EIKPGSCPEC QSTGPFSINM EQTLYRNYQK 

       370        380        390        400        410        420 
ITLQESPGRI PAGRIPRSKD VILLADLCDQ CKPGDELEVT GIYTNNYDGS LNTDQGFPVF 

       430        440        450        460        470        480 
ATVIIANHVV VKDSKQVVQS LTDEDIATIQ KLSKDPRIVE RVVASMAPSI YGHDYIKRAL 

       490        500        510        520        530        540 
ALALFGGESK NPGEKHKVRG DINLLICGDP GTAKSQFLKY TEKVAPRAVF TTGQGASAVG 

       550        560        570        580        590        600 
LTAYVRRNPV SREWTLEAGA LVLADQGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG 

       610        620        630        640        650        660 
IVTSLQARCT VIAAANPIGG RYDPSMTFSE NVNLSEPILS RFDVLCVVKD EFDPMQDQQL 

       670        680        690        700        710        720 
AKFVVHSHMK HHPSEEEQPE LEEPQLKTVD EIPQDLLRQY IVYAKENIRP KLTNIDEDKI 

       730        740        750        760        770        780 
AKMYAQLRQE SFATGSLPIT VRHIESVIRM SEAHARMHLR ENVMEADVSM AIRMMLESFI 

       790        800        810        820        830        840 
EAQKFSVMKK MRSTFQKYLS FQKDHSELLF FILRQLTLDQ LAYIRCKDGP GATHVEIMER 

       850        860        870        880 
DLIERAKQLD IVNLKPFYES DLFRTNGFSY DPKRRIILQI VVDGNTA 

« Hide

References

« Hide 'large scale' references
[1]"Cell proliferation and DNA replication defects in a Drosophila MCM2 mutant."
Treisman J.E., Follette P.J., O'Farrell P.H., Rubin G.M.
Genes Dev. 9:1709-1715(1995) [PubMed: 7622035] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Eye-antennal disk.
[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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"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: 11854416] [Abstract]
Cited for: INTERACTION WITH MCM6.
[6]"Drosophila MCM10 interacts with members of the prereplication complex and is required for proper chromosome condensation."
Christensen T.W., Tye B.K.
Mol. Biol. Cell 14:2206-2215(2003) [PubMed: 12808023] [Abstract]
Cited for: INTERACTION WITH MCM10.
[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: 16798881] [Abstract]
Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX.
[8]"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: 17372656] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26; SER-27 AND SER-124, MASS SPECTROMETRY.
[9]"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: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-92, MASS SPECTROMETRY.
Tissue: Embryo.
[10]"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: 20122406] [Abstract]
Cited for: RECONSTITUTION OF THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, MUTAGENESIS OF LYS-514.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42762 mRNA. Translation: AAB36617.1.
AE014297 Genomic DNA. Translation: AAF54207.1.
AY069702 mRNA. Translation: AAL39847.1.
RefSeqNP_477121.1. NM_057773.3.
UniGeneDm.36738.

3D structure databases

ProteinModelPortalP49735.
SMRP49735. Positions 178-781.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-22529N.
IntActP49735. 6 interactions.
MINTMINT-326578.
STRINGP49735.

Proteomic databases

PRIDEP49735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0081827; FBpp0081317; FBgn0014861.
GeneID40973.
KEGGdme:Dmel_CG7538.
NMPDRfig|7227.3.peg.11661.

Organism-specific databases

CTD4171.
FlyBaseFBgn0014861. Mcm2.

Phylogenomic databases

eggNOGinNOG08250.
GeneTreeEMGT00050000009773.
InParanoidP49735.
OMAENLEDMK.
OrthoDBEOG49S4N8.
PhylomeDBP49735.

Gene expression databases

ArrayExpressP49735.
BgeeP49735.
GermOnlineCG7538. Drosophila melanogaster.

Family and domain databases

InterProIPR008045. MCM_2.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 2 hits.
KOK02540.
PfamPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
[Graphical view]
PRINTSPR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
PROSITEPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio821540.

Entry information

Entry nameMCM2_DROME
AccessionPrimary (citable) accession number: P49735
Secondary accession number(s): Q9VHU2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families