MCM7_DROME
ID MCM7_DROME Reviewed; 720 AA.
AC Q9XYU0; P91674;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=DNA replication licensing factor Mcm7;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q61881};
DE AltName: Full=Minichromosome maintenance 7 protein;
DE Short=DmMCM3;
GN Name=Mcm7; ORFNames=CG4978;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9795205; DOI=10.1016/s0378-1119(98)00358-8;
RA Ohno K., Hirose F., Inoue Y.H., Takisawa H., Mimura S., Hashimoto Y.,
RA Kiyono T., Nishida Y., Matsukage A.;
RT "cDNA cloning and expression during development of Drosophila melanogaster
RT MCM3, MCM6 and MCM7.";
RL Gene 217:177-185(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10023044; DOI=10.1016/s0378-1119(98)00596-4;
RA Feger G.;
RT "Identification and complete cDNA sequence of the missing Drosophila MCMs:
RT DmMCM3, DmMCM6 and DmMCM7.";
RL Gene 227:149-155(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION IN THE MCM2-7 COMPLEX, AND FUNCTION OF THE MCM2-7 COMPLEX.
RX PubMed=16798881; DOI=10.1073/pnas.0602400103;
RA Moyer S.E., Lewis P.W., Botchan M.R.;
RT "Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the
RT eukaryotic DNA replication fork helicase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10236-10241(2006).
RN [7]
RP RECONSTITUTION OF THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, AND
RP MUTAGENESIS OF LYS-387 AND ARG-514.
RX PubMed=20122406; DOI=10.1016/j.molcel.2009.12.030;
RA Ilves I., Petojevic T., Pesavento J.J., Botchan M.R.;
RT "Activation of the MCM2-7 helicase by association with Cdc45 and GINS
RT proteins.";
RL Mol. Cell 37:247-258(2010).
CC -!- FUNCTION: Acts as component of the Mcm2-7 complex (Mcm complex) which
CC is the putative replicative helicase essential for 'once per cell
CC cycle' DNA replication initiation and elongation in eukaryotic cells.
CC The active ATPase sites in the Mcm2-7 ring are formed through the
CC interaction surfaces of two neighboring subunits such that a critical
CC structure of a conserved arginine finger motif is provided in trans
CC relative to the ATP-binding site of the Walker A box of the adjacent
CC subunit. The six ATPase active sites, however, are likely to contribute
CC differentially to the complex helicase activity.
CC {ECO:0000269|PubMed:16798881, ECO:0000269|PubMed:20122406}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q61881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q61881};
CC -!- SUBUNIT: Component of the Mcm2-7 complex. The complex forms a toroidal
CC hexameric ring with the proposed subunit order Mcm2-Mcm6-Mcm4-Mcm7-
CC Mcm3-Mcm5 (Probable). {ECO:0000269|PubMed:16798881, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. Specifically a MCM467 subcomplex is shown to
CC have in vitro helicase activity which is inhibited by the MCM2 subunit.
CC The MCM2-7 hexamer is the proposed physiological active complex.
CC {ECO:0000250|UniProtKB:Q61881}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34733.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB010109; BAA34733.1; ALT_SEQ; mRNA.
DR EMBL; AF124743; AAD32857.1; -; mRNA.
DR EMBL; AE014296; AAF50357.1; -; Genomic_DNA.
DR EMBL; BT001526; AAN71281.1; -; mRNA.
DR RefSeq; NP_523984.1; NM_079260.3.
DR PDB; 6RAW; EM; 3.70 A; 7=1-720.
DR PDB; 6RAX; EM; 3.99 A; 7=1-720.
DR PDB; 6RAY; EM; 4.28 A; 7=1-720.
DR PDB; 6RAZ; EM; 4.46 A; 7=1-720.
DR PDBsum; 6RAW; -.
DR PDBsum; 6RAX; -.
DR PDBsum; 6RAY; -.
DR PDBsum; 6RAZ; -.
DR AlphaFoldDB; Q9XYU0; -.
DR SMR; Q9XYU0; -.
DR BioGRID; 64419; 17.
DR ComplexPortal; CPX-2942; MCM complex.
DR DIP; DIP-59081N; -.
DR IntAct; Q9XYU0; 6.
DR STRING; 7227.FBpp0076312; -.
DR PaxDb; Q9XYU0; -.
DR PRIDE; Q9XYU0; -.
DR DNASU; 39014; -.
DR EnsemblMetazoa; FBtr0076585; FBpp0076312; FBgn0020633.
DR GeneID; 39014; -.
DR KEGG; dme:Dmel_CG4978; -.
DR UCSC; CG4978-RA; d. melanogaster.
DR CTD; 4176; -.
DR FlyBase; FBgn0020633; Mcm7.
DR VEuPathDB; VectorBase:FBgn0020633; -.
DR eggNOG; KOG0482; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q9XYU0; -.
DR OMA; NAYTCDR; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q9XYU0; -.
DR Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DME-68867; Assembly of the pre-replicative complex.
DR Reactome; R-DME-68949; Orc1 removal from chromatin.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR Reactome; R-DME-69052; Switching of origins to a post-replicative state.
DR SignaLink; Q9XYU0; -.
DR BioGRID-ORCS; 39014; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39014; -.
DR PRO; PR:Q9XYU0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0020633; Expressed in secondary oocyte and 30 other tissues.
DR ExpressionAtlas; Q9XYU0; baseline and differential.
DR Genevisible; Q9XYU0; DM.
DR GO; GO:0071162; C:CMG complex; IDA:FlyBase.
DR GO; GO:0042555; C:MCM complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR CDD; cd17758; MCM7; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008050; MCM7.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR PANTHER; PTHR11630:SF26; PTHR11630:SF26; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01663; MCMPROTEIN7.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..720
FT /note="DNA replication licensing factor Mcm7"
FT /id="PRO_0000406423"
FT DOMAIN 332..538
FT /note="MCM"
FT MOTIF 513..516
FT /note="Arginine finger"
FT BINDING 381..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 387
FT /note="K->A: Reduces complex helicase activity."
FT /evidence="ECO:0000269|PubMed:20122406"
FT MUTAGEN 514
FT /note="R->A: Reduces complex helicase activity."
FT /evidence="ECO:0000269|PubMed:20122406"
FT CONFLICT 506
FT /note="Q -> E (in Ref. 1; BAA34733)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="R -> W (in Ref. 1; BAA34733)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="S -> T (in Ref. 1; BAA34733)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="S -> T (in Ref. 1; BAA34733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 81284 MW; 09286B4D5E406756 CRC64;
MARRDYAQDR ESIKTFLSEF CKCDDDGKKE FVYGSQLVKL AHREQVLITI DLDDLAEFNE
SLAEAVVDNC RRYTSIFSDV IAELLPSYKQ QEVHAKDALD VYIEHRLMME SRTRNPMEQR
DERNSFPSEL MKRFEVGFKP LSTEKAHSIR EVKAQHIGKL VTVRGIVTRC TEVKPMMVVA
TYTCDRCGSE TYQPVNSLSF TPVHDCPSDD CRVNKAGGRL YLQTRGSKFV KFQEVKMQEH
SDQVPVGHIP RSMTIMCRGE VTRMAQPGDH IVVSGVFLPL MRTGFAQMIQ GLLSETFLQA
HRIICINKND EISDKDAELT PEELEELAQD DFYERLATSL APEIYGHLDV KKALLLLLVG
GVDKRPDGMK IRGNINICLM GDPGVAKSQL LGYISRLAVR SQYTTGRGSS GVGLTAAVMK
DPLTGEMTLE GGALVLADQG VCCIDEFDKM ADQDRTAIHE VMEQQTISIA KAGIMTTLNA
RVSILAAANP AFGRYNPRRT VEQNIQLPAA LLSRFDLLWL IQDKPDRDND LRLAKHITYV
HSHSKQPPTR VKALDMNLMR RYINLCKRKN PTIPDELTDY IVGAYVELRR EARNQKDMTF
TSARNLLGIL RLSTALARLR LSDSVEKDDV AEALRLLEMS KDSLNQIHEH QKGHVPNTSD
RIFAIVRELA GSGKAVKISD IMDRCTTKGF KPDQVDKCID DYEELNVWQV NMGRTKITFM
