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DNA replication licensing factor MCM6 (EC 3.6.4.12) (Minichromosome maintenance protein 6)

 MCM6_YEAST              Reviewed;        1017 AA.
P53091; D6VTV3; Q870M9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
18-JUL-2018, entry version 165.
RecName: Full=DNA replication licensing factor MCM6;
EC=3.6.4.12;
AltName: Full=Minichromosome maintenance protein 6;
Name=MCM6; OrderedLocusNames=YGL201C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
Duina A.A., Winston F.;
"Sequence of the Saccharomyces cerevisiae MCM6 gene.";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-766, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[4]
RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
COMPLEX, AND MUTAGENESIS OF LYS-581.
PubMed=18657510; DOI=10.1016/j.molcel.2008.05.020;
Bochman M.L., Schwacha A.;
"The Mcm2-7 complex has in vitro helicase activity.";
Mol. Cell 31:287-293(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-372, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[6]
IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX,
AND ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
PubMed=19896182; DOI=10.1016/j.cell.2009.10.015;
Remus D., Beuron F., Tolun G., Griffith J.D., Morris E.P.,
Diffley J.F.;
"Concerted loading of Mcm2-7 double hexamers around DNA during DNA
replication origin licensing.";
Cell 139:719-730(2009).
[7]
IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX,
AND ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
PubMed=19910535; DOI=10.1073/pnas.0911500106;
Evrin C., Clarke P., Zech J., Lurz R., Sun J., Uhle S., Li H.,
Stillman B., Speck C.;
"A double-hexameric MCM2-7 complex is loaded onto origin DNA during
licensing of eukaryotic DNA replication.";
Proc. Natl. Acad. Sci. U.S.A. 106:20240-20245(2009).
[8]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-1017.
STRAIN=Sigma 1278B;
PubMed=9491083; DOI=10.1007/s004380050644;
Iraqui I., Vissers S., Cartiaux M., Urrestarazu A.;
"Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes
encoding aromatic aminotransferases I and II reveals a new
aminotransferase subfamily.";
Mol. Gen. Genet. 257:238-248(1998).
[10]
INTERACTION WITH MCM10.
PubMed=9154825; DOI=10.1128/MCB.17.6.3261;
Merchant A.M., Kawasaki Y., Chen Y., Lei M., Tye B.K.;
"A lesion in the DNA replication initiation factor Mcm10 induces
pausing of elongation forks through chromosomal replication origins in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 17:3261-3271(1997).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex)
which is the putative replicative helicase essential for 'once per
cell cycle' DNA replication initiation and elongation in
eukaryotic cells. The active ATPase sites in the MCM2-7 ring are
formed through the interaction surfaces of two neighboring
subunits such that a critical structure of a conserved arginine
finger motif is provided in trans relative to the ATP-binding site
of the Walker A box of the adjacent subunit. The six ATPase active
sites, however, are likely to contribute differentially to the
complex helicase activity. Once loaded onto DNA, double hexamers
can slide on dsDNA in the absence of ATPase activity. Required for
the entry in S phase and for cell division.
{ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Component of the MCM2-7 complex. The complex forms a
toroidal hexameric ring with the proposed subunit order MCM2-MCM6-
MCM4-MCM7-MCM3-MCM5; loaded onto DNA, forms a head-head double
hexamer. Interacts with MCM10. {ECO:0000269|PubMed:19896182,
ECO:0000269|PubMed:19910535, ECO:0000269|PubMed:9154825}.
-!- INTERACTION:
P32354:MCM10; NbExp=5; IntAct=EBI-10556, EBI-5965;
P30665:MCM4; NbExp=7; IntAct=EBI-10556, EBI-4326;
Q12306:SMT3; NbExp=2; IntAct=EBI-10556, EBI-17490;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- MISCELLANEOUS: Present with 13400 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins
yielded a variety of dimeric, trimeric and tetrameric complexes
with unclear biological significance. Specifically a MCM467
subcomplex is shown to have in vitro helicase activity which is
inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed
physiological active complex.
-!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY258324; AAO89010.1; -; Genomic_DNA.
EMBL; Z72723; CAA96913.1; -; Genomic_DNA.
EMBL; Y13624; CAA73947.1; -; Genomic_DNA.
EMBL; BK006941; DAA07914.1; -; Genomic_DNA.
PIR; S64219; S64219.
RefSeq; NP_011314.2; NM_001181066.1.
PDB; 3JA8; EM; 3.80 A; 6=1-1017.
PDB; 3JC5; EM; 4.70 A; 6=1-1017.
PDB; 3JC6; EM; 3.70 A; 6=1-1017.
PDB; 3JC7; EM; 4.80 A; 6=1-1017.
PDB; 5BK4; EM; 3.90 A; 6/E=1-1017.
PDB; 5H7I; EM; 7.10 A; 6=1-1017.
PDB; 5U8S; EM; 6.10 A; 6=1-1017.
PDB; 5U8T; EM; 4.90 A; 6=1-1017.
PDB; 5UDB; EM; 3.90 A; 6=1-1017.
PDB; 5V8F; EM; 3.90 A; 6=1-1017.
PDB; 5XF8; EM; 7.10 A; 6=1-1017.
PDB; 6F0L; EM; 4.77 A; 6/E=1-1017.
PDBsum; 3JA8; -.
PDBsum; 3JC5; -.
PDBsum; 3JC6; -.
PDBsum; 3JC7; -.
PDBsum; 5BK4; -.
PDBsum; 5H7I; -.
PDBsum; 5U8S; -.
PDBsum; 5U8T; -.
PDBsum; 5UDB; -.
PDBsum; 5V8F; -.
PDBsum; 5XF8; -.
PDBsum; 6F0L; -.
ProteinModelPortal; P53091; -.
SMR; P53091; -.
BioGrid; 33056; 189.
ComplexPortal; CPX-2944; MCM complex.
DIP; DIP-1294N; -.
IntAct; P53091; 62.
MINT; P53091; -.
STRING; 4932.YGL201C; -.
iPTMnet; P53091; -.
MaxQB; P53091; -.
PaxDb; P53091; -.
PRIDE; P53091; -.
EnsemblFungi; YGL201C; YGL201C; YGL201C.
GeneID; 852673; -.
KEGG; sce:YGL201C; -.
EuPathDB; FungiDB:YGL201C; -.
SGD; S000003169; MCM6.
GeneTree; ENSGT00550000074860; -.
HOGENOM; HOG000224130; -.
InParanoid; P53091; -.
KO; K02542; -.
OMA; FLKYICS; -.
OrthoDB; EOG092C0VUM; -.
BioCyc; YEAST:G3O-30681-MONOMER; -.
Reactome; R-SCE-68949; Orc1 removal from chromatin.
Reactome; R-SCE-68962; Activation of the pre-replicative complex.
Reactome; R-SCE-69052; Switching of origins to a post-replicative state.
PRO; PR:P53091; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0071162; C:CMG complex; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0031261; C:DNA replication preinitiation complex; IDA:SGD.
GO; GO:0042555; C:MCM complex; IDA:SGD.
GO; GO:0097373; C:MCM core complex; IDA:SGD.
GO; GO:0005656; C:nuclear pre-replicative complex; IDA:SGD.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
GO; GO:0043142; F:single-stranded DNA-dependent ATPase activity; IDA:SGD.
GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD.
GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:SGD.
GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD.
InterPro; IPR031327; MCM.
InterPro; IPR008049; MCM6.
InterPro; IPR018525; MCM_CS.
InterPro; IPR001208; MCM_dom.
InterPro; IPR027925; MCM_N.
InterPro; IPR033762; MCM_OB.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11630; PTHR11630; 1.
Pfam; PF00493; MCM; 1.
Pfam; PF14551; MCM_N; 1.
Pfam; PF17207; MCM_OB; 1.
PRINTS; PR01657; MCMFAMILY.
PRINTS; PR01662; MCMPROTEIN6.
SMART; SM00350; MCM; 1.
SUPFAM; SSF50249; SSF50249; 2.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00847; MCM_1; 1.
PROSITE; PS50051; MCM_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Complete proteome;
DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 1017 DNA replication licensing factor MCM6.
/FTId=PRO_0000194117.
DOMAIN 525 732 MCM.
NP_BIND 575 582 ATP. {ECO:0000255}.
MOTIF 707 710 Arginine finger.
MOD_RES 78 78 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 766 766 Phosphothreonine.
{ECO:0000244|PubMed:17330950}.
MUTAGEN 581 581 K->A: Loss of MCM2-7 complex helicase
activity. {ECO:0000269|PubMed:18657510}.
CONFLICT 179 179 P -> A (in Ref. 2; CAA96913).
{ECO:0000305}.
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


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