MCM5_YEAST
ID MCM5_YEAST Reviewed; 775 AA.
AC P29496; D6VYS1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Minichromosome maintenance protein 5;
DE EC=3.6.4.12;
DE AltName: Full=Cell division control protein 46;
GN Name=MCM5; Synonyms=CDC46; OrderedLocusNames=YLR274W; ORFNames=L9328.1;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2044962; DOI=10.1101/gad.5.6.958;
RA Hennessy K.M., Lee A., Chen E., Botstein D.;
RT "A group of interacting yeast DNA replication genes.";
RL Genes Dev. 5:958-969(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
RP COMPLEX, AND MUTAGENESIS OF LYS-422.
RX PubMed=18657510; DOI=10.1016/j.molcel.2008.05.020;
RA Bochman M.L., Schwacha A.;
RT "The Mcm2-7 complex has in vitro helicase activity.";
RL Mol. Cell 31:287-293(2008).
RN [4]
RP IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, AND
RP ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
RX PubMed=19896182; DOI=10.1016/j.cell.2009.10.015;
RA Remus D., Beuron F., Tolun G., Griffith J.D., Morris E.P., Diffley J.F.;
RT "Concerted loading of Mcm2-7 double hexamers around DNA during DNA
RT replication origin licensing.";
RL Cell 139:719-730(2009).
RN [5]
RP IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, AND
RP ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
RX PubMed=19910535; DOI=10.1073/pnas.0911500106;
RA Evrin C., Clarke P., Zech J., Lurz R., Sun J., Uhle S., Li H., Stillman B.,
RA Speck C.;
RT "A double-hexameric MCM2-7 complex is loaded onto origin DNA during
RT licensing of eukaryotic DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20240-20245(2009).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP IDENTIFICATION OF CDC46 WITH MCM5.
RX PubMed=1438234; DOI=10.1073/pnas.89.21.10459;
RA Chen Y., Hennessy K.M., Botstein D., Tye B.-K.;
RT "CDC46/MCM5, a yeast protein whose subcellular localization is cell cycle-
RT regulated, is involved in DNA replication at autonomously replicating
RT sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10459-10463(1992).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP INTERACTION WITH CSM1.
RX PubMed=15023545; DOI=10.1016/j.yexcr.2003.12.008;
RA Wysocka M., Rytka J., Kurlandzka A.;
RT "Saccharomyces cerevisiae CSM1 gene encoding a protein influencing
RT chromosome segregation in meiosis I interacts with elements of the DNA
RT replication complex.";
RL Exp. Cell Res. 294:592-602(2004).
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; specifically the MCM2-
CC MCM5 association is proposed to be reversible and to mediate a open
CC ring conformation which may facilitate DNA loading. Once loaded onto
CC DNA, double hexamers can slide on dsDNA in the absence of ATPase
CC activity. {ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535}.
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; loaded onto DNA, forms a head-head double hexamer. Interacts
CC with CSM1. {ECO:0000269|PubMed:15023545, ECO:0000269|PubMed:19896182,
CC ECO:0000269|PubMed:19910535}.
CC -!- INTERACTION:
CC P29496; P25651: CSM1; NbExp=2; IntAct=EBI-10549, EBI-22001;
CC P29496; P24279: MCM3; NbExp=5; IntAct=EBI-10549, EBI-10541;
CC P29496; Q12306: SMT3; NbExp=3; IntAct=EBI-10549, EBI-17490;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Mobilized from the cytoplasm to the
CC nucleus as mitosis is completed. Remains in the nucleus until the
CC initiation of the next round of replication.
CC -!- MISCELLANEOUS: Present with 10300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. The MCM2-7 hexamer is the proposed
CC physiological active complex.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; U09242; AAA18027.1; -; Unassigned_DNA.
DR EMBL; U17245; AAB67364.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09587.1; -; Genomic_DNA.
DR PIR; A39631; A39631.
DR RefSeq; NP_013376.1; NM_001182161.1.
DR PDB; 3JA8; EM; 3.80 A; 5=1-775.
DR PDB; 3JC5; EM; 4.70 A; 5=1-775.
DR PDB; 3JC6; EM; 3.70 A; 5=1-775.
DR PDB; 3JC7; EM; 4.80 A; 5=1-775.
DR PDB; 5BK4; EM; 3.90 A; 5/D=1-775.
DR PDB; 5U8S; EM; 6.10 A; 5=1-775.
DR PDB; 5U8T; EM; 4.90 A; 5=1-775.
DR PDB; 5V8F; EM; 3.90 A; 5=1-775.
DR PDB; 5XF8; EM; 7.10 A; 5=1-775.
DR PDB; 6EYC; EM; 3.80 A; 5=1-775.
DR PDB; 6F0L; EM; 4.77 A; 5/D=1-775.
DR PDB; 6HV9; EM; 4.98 A; 5=1-775.
DR PDB; 6PTJ; EM; 3.80 A; 5=1-775.
DR PDB; 6PTN; EM; 5.80 A; 5/l=1-775.
DR PDB; 6PTO; EM; 7.00 A; 5/I/k=1-775.
DR PDB; 6RQC; EM; 4.40 A; 5=1-775.
DR PDB; 6SKL; EM; 3.70 A; 5=1-775.
DR PDB; 6SKO; EM; 3.40 A; 5=1-775.
DR PDB; 6U0M; EM; 3.90 A; 5=24-693.
DR PDB; 6WGF; EM; 7.70 A; 5=1-775.
DR PDB; 6WGG; EM; 8.10 A; 5=1-775.
DR PDB; 6WGI; EM; 10.00 A; 5=1-775.
DR PDB; 7P30; EM; 3.00 A; 5/D=1-775.
DR PDB; 7P5Z; EM; 3.30 A; 5/D=1-775.
DR PDB; 7PMN; EM; 3.20 A; 5=1-775.
DR PDB; 7V3U; EM; 3.20 A; 5/E=1-775.
DR PDB; 7V3V; EM; 2.90 A; 5/E=1-775.
DR PDB; 7W8G; EM; 2.52 A; 5/E=1-775.
DR PDBsum; 3JA8; -.
DR PDBsum; 3JC5; -.
DR PDBsum; 3JC6; -.
DR PDBsum; 3JC7; -.
DR PDBsum; 5BK4; -.
DR PDBsum; 5U8S; -.
DR PDBsum; 5U8T; -.
DR PDBsum; 5V8F; -.
DR PDBsum; 5XF8; -.
DR PDBsum; 6EYC; -.
DR PDBsum; 6F0L; -.
DR PDBsum; 6HV9; -.
DR PDBsum; 6PTJ; -.
DR PDBsum; 6PTN; -.
DR PDBsum; 6PTO; -.
DR PDBsum; 6RQC; -.
DR PDBsum; 6SKL; -.
DR PDBsum; 6SKO; -.
DR PDBsum; 6U0M; -.
DR PDBsum; 6WGF; -.
DR PDBsum; 6WGG; -.
DR PDBsum; 6WGI; -.
DR PDBsum; 7P30; -.
DR PDBsum; 7P5Z; -.
DR PDBsum; 7PMN; -.
DR PDBsum; 7V3U; -.
DR PDBsum; 7V3V; -.
DR PDBsum; 7W8G; -.
DR AlphaFoldDB; P29496; -.
DR SMR; P29496; -.
DR BioGRID; 31542; 276.
DR ComplexPortal; CPX-2944; MCM complex.
DR DIP; DIP-2406N; -.
DR IntAct; P29496; 81.
DR MINT; P29496; -.
DR STRING; 4932.YLR274W; -.
DR iPTMnet; P29496; -.
DR MaxQB; P29496; -.
DR PaxDb; P29496; -.
DR PRIDE; P29496; -.
DR EnsemblFungi; YLR274W_mRNA; YLR274W; YLR274W.
DR GeneID; 850980; -.
DR KEGG; sce:YLR274W; -.
DR SGD; S000004264; MCM5.
DR VEuPathDB; FungiDB:YLR274W; -.
DR eggNOG; KOG0481; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; P29496; -.
DR OMA; ITYCKTR; -.
DR BioCyc; YEAST:G3O-32373-MON; -.
DR Reactome; R-SCE-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR Reactome; R-SCE-69052; Switching of origins to a post-replicative state.
DR PRO; PR:P29496; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P29496; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0071162; C:CMG complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IPI:SGD.
DR GO; GO:0042555; C:MCM complex; IDA:SGD.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:ComplexPortal.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:SGD.
DR GO; GO:0033260; P:nuclear DNA replication; IMP:SGD.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
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; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..775
FT /note="Minichromosome maintenance protein 5"
FT /id="PRO_0000194111"
FT DOMAIN 366..573
FT /note="MCM"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 548..551
FT /note="Arginine finger"
FT BINDING 416..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 422
FT /note="K->A: Loss of MCM2-7 complex helicase activity."
FT /evidence="ECO:0000269|PubMed:18657510"
FT HELIX 351..362
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 382..393
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 423..432
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 468..471
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:6SKO"
FT TURN 480..484
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 491..499
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 551..555
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 563..576
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 596..609
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 616..635
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 650..665
FT /evidence="ECO:0007829|PDB:6SKO"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 674..685
FT /evidence="ECO:0007829|PDB:6SKO"
SQ SEQUENCE 775 AA; 86411 MW; 01D9DE208A091CF2 CRC64;
MSFDRPEIYS APVLQGESPN DDDNTEIIKS FKNFILEFRL DSQFIYRDQL RNNILVKNYS
LTVNMEHLIG YNEDIYKKLS DEPSDIIPLF ETAITQVAKR ISILSRAQSA NNNDKDPENT
SMDTDSLLLN SLPTFQLILN SNANQIPLRD LDSEHVSKIV RLSGIIISTS VLSSRATYLS
IMCRNCRHTT SITINNFNSI TGNTVSLPRS CLSTIESESS MANESNIGDE STKKNCGPDP
YIIIHESSKF IDQQFLKLQE IPELVPVGEM PRNLTMTCDR YLTNKVIPGT RVTIVGIYSI
YNSKNGAGSG RSGGGNGGSG VAIRTPYIKI LGIQSDVETS SIWNSVTMFT EEEEEEFLQL
SRNPKLYEIL TNSIAPSIFG NEDIKKAIVC LLMGGSKKIL PDGMRLRGDI NVLLLGDPGT
AKSQLLKFVE KVSPIAVYTS GKGSSAAGLT ASVQRDPMTR EFYLEGGAMV LADGGVVCID
EFDKMRDEDR VAIHEAMEQQ TISIAKAGIT TVLNSRTSVL AAANPIYGRY DDLKSPGDNI
DFQTTILSRF DMIFIVKDDH NEERDISIAN HVINIHTGNA NAMQNQQEEN GSEISIEKMK
RYITYCRLKC APRLSPQAAE KLSSNFVTIR KQLLINELES TERSSIPITI RQLEAIIRIT
ESLAKLELSP IAQERHVDEA IRLFQASTMD AASQDPIGGL NQASGTSLSE IRRFEQELKR
RLPIGWSTSY QTLRREFVDT HRFSQLALDK ALYALEKHET IQLRHQGQNI YRSGV
