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;
GN   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
//