ID   MCM6_YEAST              Reviewed;        1017 AA.
AC   P53091; D6VTV3; Q870M9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=DNA replication licensing factor MCM6;
DE            EC=3.6.4.12;
DE   AltName: Full=Minichromosome maintenance protein 6;
GN   Name=MCM6; OrderedLocusNames=YGL201C;
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].
RC   STRAIN=ATCC 204508 / S288c;
RA   Duina A.A., Winston F.;
RT   "Sequence of the Saccharomyces cerevisiae MCM6 gene.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-766, 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   [4]
RP   RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
RP   COMPLEX, AND MUTAGENESIS OF LYS-581.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-372, 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   [6]
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   [7]
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   [8]
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   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-1017.
RC   STRAIN=Sigma 1278B;
RX   PubMed=9491083; DOI=10.1007/s004380050644;
RA   Iraqui I., Vissers S., Cartiaux M., Urrestarazu A.;
RT   "Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding
RT   aromatic aminotransferases I and II reveals a new aminotransferase
RT   subfamily.";
RL   Mol. Gen. Genet. 257:238-248(1998).
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   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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, 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       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. Once loaded onto DNA,
CC       double hexamers can slide on dsDNA in the absence of ATPase activity.
CC       Required for the entry in S phase and for cell division.
CC       {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 MCM10. {ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535,
CC       ECO:0000269|PubMed:9154825}.
CC   -!- INTERACTION:
CC       P53091; P32354: MCM10; NbExp=5; IntAct=EBI-10556, EBI-5965;
CC       P53091; P30665: MCM4; NbExp=7; IntAct=EBI-10556, EBI-4326;
CC       P53091; Q12306: SMT3; NbExp=2; IntAct=EBI-10556, EBI-17490;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 13400 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. 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; AY258324; AAO89010.1; -; Genomic_DNA.
DR   EMBL; Z72723; CAA96913.1; -; Genomic_DNA.
DR   EMBL; Y13624; CAA73947.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07914.1; -; Genomic_DNA.
DR   PIR; S64219; S64219.
DR   RefSeq; NP_011314.2; NM_001181066.1.
DR   PDB; 3JA8; EM; 3.80 A; 6=1-1017.
DR   PDB; 3JC5; EM; 4.70 A; 6=1-1017.
DR   PDB; 3JC6; EM; 3.70 A; 6=1-1017.
DR   PDB; 3JC7; EM; 4.80 A; 6=1-1017.
DR   PDB; 5BK4; EM; 3.90 A; 6/E=1-1017.
DR   PDB; 5U8S; EM; 6.10 A; 6=1-1017.
DR   PDB; 5U8T; EM; 4.90 A; 6=1-1017.
DR   PDB; 5V8F; EM; 3.90 A; 6=1-1017.
DR   PDB; 5XF8; EM; 7.10 A; 6=1-1017.
DR   PDB; 6EYC; EM; 3.80 A; 6=1-1017.
DR   PDB; 6F0L; EM; 4.77 A; 6/E=1-1017.
DR   PDB; 6HV9; EM; 4.98 A; 6=1-1017.
DR   PDB; 6PTJ; EM; 3.80 A; 6=1-1017.
DR   PDB; 6PTN; EM; 5.80 A; 6/m=1-1017.
DR   PDB; 6PTO; EM; 7.00 A; 6/J/l=1-1017.
DR   PDB; 6RQC; EM; 4.40 A; 6=1-1017.
DR   PDB; 6SKL; EM; 3.70 A; 6=1-1017.
DR   PDB; 6SKO; EM; 3.40 A; 6=1-1017.
DR   PDB; 6U0M; EM; 3.90 A; 6=103-840.
DR   PDB; 6WGF; EM; 7.70 A; 6=1-1017.
DR   PDB; 6WGG; EM; 8.10 A; 6=1-1017.
DR   PDB; 6WGI; EM; 10.00 A; 6=1-1017.
DR   PDB; 7P30; EM; 3.00 A; 6/E=1-1017.
DR   PDB; 7P5Z; EM; 3.30 A; 6/E=1-1017.
DR   PDB; 7PMK; EM; 3.20 A; 6=1-1017.
DR   PDB; 7PMN; EM; 3.20 A; 6=1-1017.
DR   PDB; 7PT6; EM; 3.20 A; 6/F=1-1017.
DR   PDB; 7PT7; EM; 3.80 A; 6/F=1-1017.
DR   PDB; 7QHS; EM; 3.30 A; 6=1-1017.
DR   PDB; 7V3U; EM; 3.20 A; 6/F=1-1017.
DR   PDB; 7V3V; EM; 2.90 A; 6/F=1-1017.
DR   PDB; 7W8G; EM; 2.52 A; 6/F=1-1017.
DR   PDB; 7Z13; EM; 3.40 A; 6/e=1-1017.
DR   PDB; 8B9A; EM; 3.50 A; 6=1-1017.
DR   PDB; 8B9B; EM; 3.50 A; 6=1-1017.
DR   PDB; 8B9C; EM; 4.60 A; 6=1-1017.
DR   PDB; 8KG6; EM; 3.07 A; 6=1-1017.
DR   PDB; 8KG8; EM; 4.23 A; 6=1-1017.
DR   PDB; 8KG9; EM; 4.52 A; 6=1-1017.
DR   PDB; 8W7M; EM; 4.12 A; 6=1-1017.
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; 7PMK; -.
DR   PDBsum; 7PMN; -.
DR   PDBsum; 7PT6; -.
DR   PDBsum; 7PT7; -.
DR   PDBsum; 7QHS; -.
DR   PDBsum; 7V3U; -.
DR   PDBsum; 7V3V; -.
DR   PDBsum; 7W8G; -.
DR   PDBsum; 7Z13; -.
DR   PDBsum; 8B9A; -.
DR   PDBsum; 8B9B; -.
DR   PDBsum; 8B9C; -.
DR   PDBsum; 8KG6; -.
DR   PDBsum; 8KG8; -.
DR   PDBsum; 8KG9; -.
DR   PDBsum; 8W7M; -.
DR   AlphaFoldDB; P53091; -.
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-14439; -.
DR   EMDB; EMD-15924; -.
DR   EMDB; EMD-20471; -.
DR   EMDB; EMD-20472; -.
DR   EMDB; EMD-20473; -.
DR   EMDB; EMD-20607; -.
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; P53091; -.
DR   BioGRID; 33056; 213.
DR   ComplexPortal; CPX-2944; MCM complex.
DR   DIP; DIP-1294N; -.
DR   IntAct; P53091; 59.
DR   MINT; P53091; -.
DR   STRING; 4932.YGL201C; -.
DR   GlyGen; P53091; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P53091; -.
DR   MaxQB; P53091; -.
DR   PaxDb; 4932-YGL201C; -.
DR   PeptideAtlas; P53091; -.
DR   EnsemblFungi; YGL201C_mRNA; YGL201C; YGL201C.
DR   GeneID; 852673; -.
DR   KEGG; sce:YGL201C; -.
DR   AGR; SGD:S000003169; -.
DR   SGD; S000003169; MCM6.
DR   VEuPathDB; FungiDB:YGL201C; -.
DR   eggNOG; KOG0480; Eukaryota.
DR   GeneTree; ENSGT01050000244824; -.
DR   HOGENOM; CLU_000995_3_0_1; -.
DR   InParanoid; P53091; -.
DR   OMA; CQTEIRN; -.
DR   OrthoDB; 5476523at2759; -.
DR   BioCyc; YEAST:G3O-30681-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; 852673; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P53091; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53091; Protein.
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; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:SGD.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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:1902969; P:mitotic DNA replication; IBA:GO_Central.
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   CDD; cd17757; MCM6; 1.
DR   Gene3D; 1.20.58.870; -; 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; IPR031327; MCM.
DR   InterPro; IPR008049; MCM6.
DR   InterPro; IPR041024; Mcm6_C.
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:SF43; DNA REPLICATION LICENSING FACTOR MCM6; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF18263; MCM6_C; 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; PR01662; MCMPROTEIN6.
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; DNA replication; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1017
FT                   /note="DNA replication licensing factor MCM6"
FT                   /id="PRO_0000194117"
FT   DOMAIN          525..732
FT                   /note="MCM"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          852..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           707..710
FT                   /note="Arginine finger"
FT   COMPBIAS        1..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         575..582
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         766
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MUTAGEN         581
FT                   /note="K->A: Loss of MCM2-7 complex helicase activity."
FT                   /evidence="ECO:0000269|PubMed:18657510"
FT   CONFLICT        179
FT                   /note="P -> A (in Ref. 2; CAA96913)"
FT                   /evidence="ECO:0000305"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           106..121
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           135..145
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           155..160
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           161..164
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           165..172
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           174..192
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           194..197
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          264..268
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          286..297
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          301..314
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          317..322
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            348..350
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          351..362
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            365..367
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          369..371
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          376..382
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           383..385
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          394..405
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            407..410
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            441..445
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          450..461
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           501..505
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           510..520
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           525..532
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           541..551
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          571..575
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           582..591
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          592..599
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            600..602
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           605..608
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          609..613
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          622..625
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           627..630
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            631..633
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          634..639
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           641..643
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           646..650
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           653..657
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          659..665
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          668..673
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          676..681
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            695..698
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           703..706
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          709..715
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           721..734
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           738..740
FT                   /evidence="ECO:0007829|PDB:6SKO"
FT   HELIX           748..758
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           767..784
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            787..790
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           797..813
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          817..819
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           821..835
FT                   /evidence="ECO:0007829|PDB:7PMK"
SQ   SEQUENCE   1017 AA;  112978 MW;  03AB793134E64A50 CRC64;
     MSSPFPADTP SSNRPSNSSP PPSSIGAGFG SSSGLDSQIG SRLHFPSSSQ PHVSNSQTGP
     FVNDSTQFSS QRLQTDGSAT NDMEGNEPAR SFKSRALNHV KKVDDVTGEK VREAFEQFLE
     DFSVQSTDTG EVEKVYRAQI EFMKIYDLNT IYIDYQHLSM RENGALAMAI SEQYYRFLPF
     LQKGLRRVVR KYAPELLNTS DSLKRSEGDE GQADEDEQQD DDMNGSSLPR DSGSSAAPGN
     GTSAMATRSI TTSTSPEQTE RVFQISFFNL PTVHRIRDIR SEKIGSLLSI SGTVTRTSEV
     RPELYKASFT CDMCRAIVDN VEQSFKYTEP TFCPNPSCEN RAFWTLNVTR SRFLDWQKVR
     IQENANEIPT GSMPRTLDVI LRGDSVERAK PGDRCKFTGV EIVVPDVTQL GLPGVKPSST
     LDTRGISKTT EGLNSGVTGL RSLGVRDLTY KISFLACHVI SIGSNIGASS PDANSNNRET
     ELQMAANLQA NNVYQDNERD QEVFLNSLSS DEINELKEMV KDEHIYDKLV RSIAPAVFGH
     EAVKKGILLQ MLGGVHKSTV EGIKLRGDIN ICVVGDPSTS KSQFLKYVVG FAPRSVYTSG
     KASSAAGLTA AVVRDEEGGD YTIEAGALML ADNGICCIDE FDKMDISDQV AIHEAMEQQT
     ISIAKAGIHA TLNARTSILA AANPVGGRYN RKLSLRGNLN MTAPIMSRFD LFFVILDDCN
     EKIDTELASH IVDLHMKRDE AIEPPFSAEQ LRRYIKYART FKPILTKEAR SYLVEKYKEL
     RKDDAQGFSR SSYRITVRQL ESMIRLSEAI ARANCVDEIT PSFIAEAYDL LRQSIIRVDV
     DDVEMDEEFD NIESQSHAAS GNNDDNDDGT GSGVITSEPP ADIEEGQSEA TARPGTSEKK
     KTTVTYDKYV SMMNMIVRKI AEVDREGAEE LTAVDIVDWY LLQKENDLGS LAEYWEERRL
     AFKVIKRLVK DRILMEIHGT RHNLRDLENE ENENNKTVYV IHPNCEVLDQ LEPQDSS
//