ID MCM7_YEAST Reviewed; 845 AA.
AC P38132; D6VQK0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 27-MAR-2024, entry version 217.
DE RecName: Full=DNA replication licensing factor MCM7;
DE EC=3.6.4.12;
DE AltName: Full=Cell division control protein 47;
DE AltName: Full=Minichromosome maintenance protein 7;
GN Name=MCM7; Synonyms=CDC47; OrderedLocusNames=YBR202W; ORFNames=YBR1441;
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 [GENOMIC DNA].
RX PubMed=7708676; DOI=10.1073/pnas.92.7.2514;
RA Dalton S., Whitbread L.;
RT "Cell cycle-regulated nuclear import and export of Cdc47, a protein
RT essential for initiation of DNA replication in budding yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2514-2518(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8368014; DOI=10.1002/yea.320090714;
RA Bussereau F., Mallet L., Gaillon L., Jacquet M.;
RT "A 12.8 kb segment, on the right arm of chromosome II from Saccharomyces
RT cerevisiae including part of the DUR1,2 gene, contains five putative new
RT genes.";
RL Yeast 9:797-806(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 552; 556-558 AND 574.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-811, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
RP COMPLEX, AND MUTAGENESIS OF LYS-466.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-811 AND SER-819, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
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 [9]
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 [10]
RP INTERACTION WITH MCM10.
RX PubMed=9154825; DOI=10.1128/mcb.17.6.3261;
RA Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K.;
RT "A lesion in the DNA replication initiation factor Mcm10 induces pausing of
RT elongation forks through chromosomal replication origins in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 17:3261-3271(1997).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
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 [13]
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).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-838, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Acts as a 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 Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine
CC that unwinds template DNA during replication, and around which the
CC replisome is built. The active ATPase sites in the MCM2-7 ring are
CC formed through the interaction surfaces of two neighboring subunits
CC such that a critical structure of a conserved arginine finger motif is
CC provided in trans relative to the ATP-binding site of the Walker A box
CC of the adjacent subunit. The six ATPase active sites, however, are
CC likely to contribute differentially to the complex helicase activity.
CC Once loaded onto DNA, double hexamers can slide on dsDNA in the absence
CC of ATPase activity. {ECO:0000269|PubMed:19896182,
CC 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 Evidence={ECO:0000250|UniProtKB:P33993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P33993};
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 and MCM10. {ECO:0000269|PubMed:15023545,
CC ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535,
CC ECO:0000269|PubMed:9154825}.
CC -!- INTERACTION:
CC P38132; P25651: CSM1; NbExp=3; IntAct=EBI-4300, EBI-22001;
CC P38132; P53199: ERG26; NbExp=2; IntAct=EBI-4300, EBI-6514;
CC P38132; P24279: MCM3; NbExp=2; IntAct=EBI-4300, EBI-10541;
CC P38132; P30665: MCM4; NbExp=3; IntAct=EBI-4300, EBI-4326;
CC P38132; Q12306: SMT3; NbExp=2; IntAct=EBI-4300, EBI-17490;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 166 molecules/cell in log phase SD medium.
CC {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. 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 -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; U14730; AAA86309.1; -; Genomic_DNA.
DR EMBL; Z21487; CAA79689.1; -; Genomic_DNA.
DR EMBL; Z36071; CAA85166.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07320.2; -; Genomic_DNA.
DR PIR; S34027; S34027.
DR RefSeq; NP_009761.4; NM_001178550.4.
DR PDB; 3JA8; EM; 3.80 A; 7=1-845.
DR PDB; 3JC5; EM; 4.70 A; 7=1-845.
DR PDB; 3JC6; EM; 3.70 A; 7=1-845.
DR PDB; 3JC7; EM; 4.80 A; 7=1-845.
DR PDB; 5BK4; EM; 3.90 A; 7/F=1-845.
DR PDB; 5U8S; EM; 6.10 A; 7=1-845.
DR PDB; 5U8T; EM; 4.90 A; 7=1-845.
DR PDB; 5V8F; EM; 3.90 A; 7=1-800.
DR PDB; 5XF8; EM; 7.10 A; 7=1-845.
DR PDB; 6EYC; EM; 3.80 A; 7=1-845.
DR PDB; 6F0L; EM; 4.77 A; 7/F=1-845.
DR PDB; 6HV9; EM; 4.98 A; 7=1-845.
DR PDB; 6PTJ; EM; 3.80 A; 7=1-845.
DR PDB; 6PTN; EM; 5.80 A; 7/n=1-845.
DR PDB; 6PTO; EM; 7.00 A; 7/K/m=1-845.
DR PDB; 6RQC; EM; 4.40 A; 7=1-845.
DR PDB; 6SKL; EM; 3.70 A; 7=1-845.
DR PDB; 6SKO; EM; 3.40 A; 7=1-845.
DR PDB; 6U0M; EM; 3.90 A; 7=1-729.
DR PDB; 6WGC; EM; 4.30 A; 7=1-845.
DR PDB; 6WGF; EM; 7.70 A; 7=1-845.
DR PDB; 6WGG; EM; 8.10 A; 7=1-845.
DR PDB; 6WGI; EM; 10.00 A; 7=1-845.
DR PDB; 7P30; EM; 3.00 A; 7/F=1-845.
DR PDB; 7P5Z; EM; 3.30 A; 7/F=1-845.
DR PDB; 7PMK; EM; 3.20 A; 7=1-845.
DR PDB; 7PMN; EM; 3.20 A; 7=1-845.
DR PDB; 7PT6; EM; 3.20 A; 7/G=1-845.
DR PDB; 7PT7; EM; 3.80 A; 7/G=1-845.
DR PDB; 7QHS; EM; 3.30 A; 7=1-845.
DR PDB; 7V3U; EM; 3.20 A; 7/G=1-845.
DR PDB; 7V3V; EM; 2.90 A; 7/G=1-845.
DR PDB; 7W8G; EM; 2.52 A; 7/G=1-845.
DR PDB; 8B9A; EM; 3.50 A; 7=1-845.
DR PDB; 8B9B; EM; 3.50 A; 7=1-845.
DR PDB; 8B9C; EM; 4.60 A; 7=1-845.
DR PDB; 8KG6; EM; 3.07 A; 7=1-845.
DR PDB; 8KG8; EM; 4.23 A; 7=1-845.
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; 6WGC; -.
DR PDBsum; 6WGF; -.
DR PDBsum; 6WGG; -.
DR PDBsum; 6WGI; -.
DR PDBsum; 7P30; -.
DR PDBsum; 7P5Z; -.
DR PDBsum; 7PMK; -.
DR PDBsum; 7PMN; -.
DR PDBsum; 7PT6; -.
DR PDBsum; 7PT7; -.
DR PDBsum; 7QHS; -.
DR PDBsum; 7V3U; -.
DR PDBsum; 7V3V; -.
DR PDBsum; 7W8G; -.
DR PDBsum; 8B9A; -.
DR PDBsum; 8B9B; -.
DR PDBsum; 8B9C; -.
DR PDBsum; 8KG6; -.
DR PDBsum; 8KG8; -.
DR AlphaFoldDB; P38132; -.
DR EMDB; EMD-0288; -.
DR EMDB; EMD-10227; -.
DR EMDB; EMD-10230; -.
DR EMDB; EMD-13176; -.
DR EMDB; EMD-13211; -.
DR EMDB; EMD-13537; -.
DR EMDB; EMD-13539; -.
DR EMDB; EMD-13619; -.
DR EMDB; EMD-13620; -.
DR EMDB; EMD-13978; -.
DR EMDB; EMD-15924; -.
DR EMDB; EMD-20471; -.
DR EMDB; EMD-20472; -.
DR EMDB; EMD-20473; -.
DR EMDB; EMD-20607; -.
DR EMDB; EMD-21662; -.
DR EMDB; EMD-21664; -.
DR EMDB; EMD-21665; -.
DR EMDB; EMD-21666; -.
DR EMDB; EMD-31684; -.
DR EMDB; EMD-31685; -.
DR EMDB; EMD-32355; -.
DR EMDB; EMD-4980; -.
DR EMDB; EMD-6671; -.
DR EMDB; EMD-8518; -.
DR EMDB; EMD-8519; -.
DR EMDB; EMD-8540; -.
DR EMDB; EMD-9400; -.
DR SMR; P38132; -.
DR BioGRID; 32899; 414.
DR ComplexPortal; CPX-2944; MCM complex.
DR DIP; DIP-2408N; -.
DR IntAct; P38132; 14.
DR MINT; P38132; -.
DR STRING; 4932.YBR202W; -.
DR iPTMnet; P38132; -.
DR MaxQB; P38132; -.
DR PaxDb; 4932-YBR202W; -.
DR PeptideAtlas; P38132; -.
DR EnsemblFungi; YBR202W_mRNA; YBR202W; YBR202W.
DR GeneID; 852501; -.
DR KEGG; sce:YBR202W; -.
DR AGR; SGD:S000000406; -.
DR SGD; S000000406; MCM7.
DR VEuPathDB; FungiDB:YBR202W; -.
DR eggNOG; KOG0482; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; P38132; -.
DR OMA; AQHVTYV; -.
DR OrthoDB; 5476523at2759; -.
DR BioCyc; YEAST:G3O-29143-MONOMER; -.
DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SCE-68867; Assembly of the pre-replicative complex.
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 BioGRID-ORCS; 852501; 0 hits in 10 CRISPR screens.
DR PRO; PR:P38132; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38132; Protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
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; IDA:SGD.
DR GO; GO:0042555; C:MCM complex; IDA:SGD.
DR GO; GO:0097373; C:MCM core 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; IDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:1904931; F:MCM complex binding; IDA:SGD.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; 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:0006279; P:premeiotic DNA replication; IDA:ComplexPortal.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD.
DR CDD; cd17758; MCM7; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF26; DNA REPLICATION LICENSING FACTOR MCM7; 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; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Phosphoprotein; Reference proteome.
FT CHAIN 1..845
FT /note="DNA replication licensing factor MCM7"
FT /id="PRO_0000194124"
FT DOMAIN 410..617
FT /note="MCM"
FT REGION 812..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 592..595
FT /note="Arginine finger"
FT COMPBIAS 813..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared with MCM3"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT BINDING 463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared with MCM3"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT BINDING 465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared with MCM3"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT BINDING 466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared with MCM3"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT BINDING 467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared with MCM3"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT BINDING 568
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared with MCM3"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT BINDING 687
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 811
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 466
FT /note="K->A: Loss of MCM2-7 complex helicase activity."
FT /evidence="ECO:0000269|PubMed:18657510"
FT CONFLICT 552
FT /note="G -> V (in Ref. 2; CAA79689 and 3; CAA85166)"
FT /evidence="ECO:0000305"
FT CONFLICT 556..558
FT /note="TLN -> NPG (in Ref. 2; CAA79689 and 3; CAA85166)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="Y -> I (in Ref. 2; CAA79689 and 3; CAA85166)"
FT /evidence="ECO:0000305"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 138..154
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 237..248
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 252..262
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 297..316
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 348..358
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 373..383
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 397..407
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 467..476
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 490..494
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 512..515
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 531..543
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 580..583
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 588..591
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 608..622
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 635..647
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 654..671
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 677..679
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 686..702
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 710..726
FT /evidence="ECO:0007829|PDB:7PMK"
SQ SEQUENCE 845 AA; 94943 MW; ADA66C719D96DB4A CRC64;
MSAALPSIQL PVDYNNLFNE ITDFLVTFKQ DTLSSDATRN ENEDENLDAE NIEQHLLEKG
PKYMAMLQKV ANRELNSVII DLDDILQYQN EKFLQGTQAD DLVSAIQQNA NHFTELFCRA
IDNNMPLPTK EIDYKDDVLD VILNQRRLRN ERMLSDRTNE IRSENLMDTT MDPPSSMNDA
LREVVEDETE LFPPNLTRRY FLYFKPLSQN CARRYRKKAI SSKPLSVRQI KGDFLGQLIT
VRGIITRVSD VKPAVEVIAY TCDQCGYEVF QEVNSRTFTP LSECTSEECS QNQTKGQLFM
STRASKFSAF QECKIQELSQ QVPVGHIPRS LNIHVNGTLV RSLSPGDIVD VTGIFLPAPY
TGFKALKAGL LTETYLEAQF VRQHKKKFAS FSLTSDVEER VMELITSGDV YNRLAKSIAP
EIYGNLDVKK ALLLLLVGGV DKRVGDGMKI RGDINVCLMG DPGVAKSQLL KAICKISPRG
VYTTGKGSSG VGLTAAVMKD PVTDEMILEG GALVLADNGI CCIDEFDKMD ESDRTAIHEV
MEQQTISISK AGINTTLNAR TSILAAANPL YGRYNPRLSP LDNINLPAAL LSRFDILFLM
LDIPSRDDDE KLAEHVTYVH MHNKQPDLDF TPVEPSKMRE YIAYAKTKRP VMSEAVNDYV
VQAYIRLRQD SKREMDSKFS FGQATPRTLL GIIRLSQALA KLRLADMVDI DDVEEALRLV
RVSKESLYQE TNKSKEDESP TTKIFTIIKK MLQETGKNTL SYENIVKTVR LRGFTMLQLS
NCIQEYSYLN VWHLINEGNT LKFVDDGTMD TDQEDSLVST PKLAPQTTAS ANVSAQDSDI
DLQDA
//
