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DNA replication licensing factor MCM7 (EC 3.6.4.12) (Cell division control protein 47) (Minichromosome maintenance protein 7)

 MCM7_YEAST              Reviewed;         845 AA.
P38132; D6VQK0;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
18-JUL-2018, entry version 183.
RecName: Full=DNA replication licensing factor MCM7;
EC=3.6.4.12;
AltName: Full=Cell division control protein 47;
AltName: Full=Minichromosome maintenance protein 7;
Name=MCM7; Synonyms=CDC47; OrderedLocusNames=YBR202W;
ORFNames=YBR1441;
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].
PubMed=7708676; DOI=10.1073/pnas.92.7.2514;
Dalton S., Whitbread L.;
"Cell cycle-regulated nuclear import and export of Cdc47, a protein
essential for initiation of DNA replication in budding yeast.";
Proc. Natl. Acad. Sci. U.S.A. 92:2514-2518(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8368014; DOI=10.1002/yea.320090714;
Bussereau F., Mallet L., Gaillon L., Jacquet M.;
"A 12.8 kb segment, on the right arm of chromosome II from
Saccharomyces cerevisiae including part of the DUR1,2 gene, contains
five putative new genes.";
Yeast 9:797-806(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
GENOME REANNOTATION, AND SEQUENCE REVISION TO 552; 556-558 AND 574.
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-811, 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).
[6]
RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
COMPLEX, AND MUTAGENESIS OF LYS-466.
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-811 AND SER-819, 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).
[8]
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).
[9]
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).
[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]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[12]
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).
[13]
INTERACTION WITH CSM1.
PubMed=15023545; DOI=10.1016/j.yexcr.2003.12.008;
Wysocka M., Rytka J., Kurlandzka A.;
"Saccharomyces cerevisiae CSM1 gene encoding a protein influencing
chromosome segregation in meiosis I interacts with elements of the DNA
replication complex.";
Exp. Cell Res. 294:592-602(2004).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-838, 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.
{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 CSM1 and MCM10.
{ECO:0000269|PubMed:15023545, ECO:0000269|PubMed:19896182,
ECO:0000269|PubMed:19910535, ECO:0000269|PubMed:9154825}.
-!- INTERACTION:
P25651:CSM1; NbExp=3; IntAct=EBI-4300, EBI-22001;
P53199:ERG26; NbExp=2; IntAct=EBI-4300, EBI-6514;
P24279:MCM3; NbExp=2; IntAct=EBI-4300, EBI-10541;
P30665:MCM4; NbExp=3; IntAct=EBI-4300, EBI-4326;
Q12306:SMT3; NbExp=2; IntAct=EBI-4300, EBI-17490;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 166 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; U14730; AAA86309.1; -; Genomic_DNA.
EMBL; Z21487; CAA79689.1; -; Genomic_DNA.
EMBL; Z36071; CAA85166.1; -; Genomic_DNA.
EMBL; BK006936; DAA07320.2; -; Genomic_DNA.
PIR; S34027; S34027.
RefSeq; NP_009761.4; NM_001178550.4.
PDB; 3JA8; EM; 3.80 A; 7=1-845.
PDB; 3JC5; EM; 4.70 A; 7=1-845.
PDB; 3JC6; EM; 3.70 A; 7=1-845.
PDB; 3JC7; EM; 4.80 A; 7=1-845.
PDB; 5BK4; EM; 3.90 A; 7/F=1-845.
PDB; 5H7I; EM; 7.10 A; 7=1-845.
PDB; 5U8S; EM; 6.10 A; 7=1-845.
PDB; 5U8T; EM; 4.90 A; 7=1-845.
PDB; 5UDB; EM; 3.90 A; 7=1-845.
PDB; 5V8F; EM; 3.90 A; 7=1-800.
PDB; 5XF8; EM; 7.10 A; 7=1-845.
PDB; 6F0L; EM; 4.77 A; 7/F=1-845.
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; P38132; -.
SMR; P38132; -.
BioGrid; 32899; 404.
ComplexPortal; CPX-2944; MCM complex.
DIP; DIP-2408N; -.
IntAct; P38132; 18.
MINT; P38132; -.
STRING; 4932.YBR202W; -.
iPTMnet; P38132; -.
MaxQB; P38132; -.
PaxDb; P38132; -.
PRIDE; P38132; -.
EnsemblFungi; YBR202W; YBR202W; YBR202W.
GeneID; 852501; -.
KEGG; sce:YBR202W; -.
EuPathDB; FungiDB:YBR202W; -.
SGD; S000000406; MCM7.
GeneTree; ENSGT00920000149094; -.
InParanoid; P38132; -.
KO; K02210; -.
OMA; VKIQEMA; -.
OrthoDB; EOG092C0VUM; -.
BioCyc; YEAST:G3O-29143-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:P38132; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
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; IDA:SGD.
GO; GO:0003682; F:chromatin binding; IDA:SGD.
GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
GO; GO:1904931; F:MCM complex binding; IDA:SGD.
GO; GO:0043142; F:single-stranded DNA-dependent ATPase activity; IDA:SGD.
GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
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:0033260; P:nuclear DNA replication; IMP:SGD.
GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR031327; MCM.
InterPro; IPR008050; MCM7.
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.
PANTHER; PTHR11630:SF26; PTHR11630:SF26; 1.
Pfam; PF00493; MCM; 1.
Pfam; PF14551; MCM_N; 1.
Pfam; PF17207; MCM_OB; 1.
PRINTS; PR01657; MCMFAMILY.
PRINTS; PR01663; MCMPROTEIN7.
SMART; SM00382; AAA; 1.
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; Cytoplasm;
DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 845 DNA replication licensing factor MCM7.
/FTId=PRO_0000194124.
DOMAIN 410 617 MCM.
NP_BIND 460 467 ATP. {ECO:0000255}.
MOTIF 592 595 Arginine finger.
MOD_RES 811 811 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956}.
MOD_RES 819 819 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 466 466 K->A: Loss of MCM2-7 complex helicase
activity. {ECO:0000269|PubMed:18657510}.
CONFLICT 552 552 G -> V (in Ref. 2; CAA79689 and 3;
CAA85166). {ECO:0000305}.
CONFLICT 556 558 TLN -> NPG (in Ref. 2; CAA79689 and 3;
CAA85166). {ECO:0000305}.
CONFLICT 574 574 Y -> I (in Ref. 2; CAA79689 and 3;
CAA85166). {ECO:0000305}.
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


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