MCM5_DROME
ID MCM5_DROME Reviewed; 733 AA.
AC Q9VGW6; P91676;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=DNA replication licensing factor Mcm5;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance 5 protein;
DE Short=DmMCM5;
GN Name=Mcm5; ORFNames=CG4082;
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=9224901; DOI=10.1016/s0378-1119(97)00107-8;
RA Su T.T., Yakubovich N., O'Farrell P.H.;
RT "Cloning of Drosophila MCM homologs and analysis of their requirement
RT during embryogenesis.";
RL Gene 192:283-289(1997).
RN [2]
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 [3]
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 [4]
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 (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP RECONSTITUTION OF THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, AND
RP MUTAGENESIS OF LYS-384.
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 -!- 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 -!- INTERACTION:
CC Q9VGW6; P49735: Mcm2; NbExp=9; IntAct=EBI-83298, EBI-138228;
CC Q9VGW6; Q9XYU1: Mcm3; NbExp=7; IntAct=EBI-83298, EBI-103930;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P33992}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P33992}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC47652.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U83493; AAC47652.1; ALT_FRAME; mRNA.
DR EMBL; AE014297; AAF54557.1; -; Genomic_DNA.
DR EMBL; AY071628; AAL49250.1; -; mRNA.
DR RefSeq; NP_524308.2; NM_079584.4.
DR PDB; 6RAW; EM; 3.70 A; 5=1-733.
DR PDB; 6RAX; EM; 3.99 A; 5=1-733.
DR PDB; 6RAY; EM; 4.28 A; 5=1-733.
DR PDB; 6RAZ; EM; 4.46 A; 5=1-733.
DR PDBsum; 6RAW; -.
DR PDBsum; 6RAX; -.
DR PDBsum; 6RAY; -.
DR PDBsum; 6RAZ; -.
DR AlphaFoldDB; Q9VGW6; -.
DR SMR; Q9VGW6; -.
DR BioGRID; 66440; 21.
DR ComplexPortal; CPX-2942; MCM complex.
DR IntAct; Q9VGW6; 19.
DR STRING; 7227.FBpp0081756; -.
DR PaxDb; Q9VGW6; -.
DR PRIDE; Q9VGW6; -.
DR EnsemblMetazoa; FBtr0082279; FBpp0081756; FBgn0017577.
DR GeneID; 41296; -.
DR KEGG; dme:Dmel_CG4082; -.
DR UCSC; CG4082-RA; d. melanogaster.
DR CTD; 4174; -.
DR FlyBase; FBgn0017577; Mcm5.
DR VEuPathDB; VectorBase:FBgn0017577; -.
DR eggNOG; KOG0481; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q9VGW6; -.
DR OMA; ITYCKTR; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q9VGW6; -.
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; Q9VGW6; -.
DR BioGRID-ORCS; 41296; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41296; -.
DR PRO; PR:Q9VGW6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0017577; Expressed in secondary oocyte and 40 other tissues.
DR Genevisible; Q9VGW6; DM.
DR GO; GO:0071162; C:CMG complex; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:FlyBase.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IMP:FlyBase.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008048; MCM5.
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 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; PR01661; MCMPROTEIN5.
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; Cytoplasm; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..733
FT /note="DNA replication licensing factor Mcm5"
FT /id="PRO_0000406422"
FT DOMAIN 328..534
FT /note="MCM"
FT MOTIF 509..512
FT /note="Arginine finger"
FT BINDING 378..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 384
FT /note="K->A: Greatly reduces complex helicase activity."
FT /evidence="ECO:0000269|PubMed:20122406"
FT CONFLICT 302
FT /note="A -> V (in Ref. 2; AAC47652)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="F -> L (in Ref. 2; AAC47652)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="G -> V (in Ref. 2; AAC47652)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="M -> V (in Ref. 2; AAC47652)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 733 AA; 82258 MW; 36FEB693045A30B8 CRC64;
MEGFDDAGVF FSDNFGGDNQ QDAQINLQAV KKKYKEFIRT FNEENFFYKY RDTLKRNYLN
GRYFLEIEME DLVGFDETLA DKLNKQPTEH LEIFEEAARE VADEITAPRP EHEEHMHDIQ
ILLSSNANPT NIRQLKSDCV SKLVKIAGII VAASGISAKA TRMSIQCLSC STVIPNLKVN
PGLEGYALPR KCNTEQAGRP KCPLDPFFIM PDKCKCVDFQ TLKLQELPDF VPQGEIPRHL
QLFCDRSLCE RVVPGNRVLI QGIYSIRKVG KPSRRDGREK AVVGVRAPYM RVVGITVDSE
GAGAISRYSN ITSDEEEHFR RMAASGDIYE RLSQSLAPSI FGSRDIKKAI TCMLFGGSRK
RLPDGLCRRG DINVLLLGDP GTAKSQLLKF VEKVAPIAVY TSGKGSSAAG LTASVMKDPQ
TRNFVMEGGA MVLADGGVVC IDEFDKMRED DRVAIHEAME QQTISIAKAG ITTTLNSRCS
VLAAANSIFG RWDDTKGEEN IDFMPTILSR FDMIFIVKDI HDESRDITLA KHIINVHLSS
NKSAPSEPAE GEISLSTFKK YIHYCRTHCG PRLSEAAGEK LKSRYVLMRS GAGQQEKASD
KRLSIPITVR QLEAVIRISE SLAKIRLQPF ATDEHVNEAL RLFQVSTLDA AMTGSLAGAE
GFTTEEDQET LNRIEKQLKR RFAIGSQVSE QNILQDFLRQ KYEERTVMKV IHTMIRRGEL
QHRMQRKMLY RIC
