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DNA replication licensing factor MCM4 (EC 3.6.4.12) (Cell division control protein 54)

 MCM4_YEAST              Reviewed;         933 AA.
P30665; D6W429;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
12-SEP-2018, entry version 180.
RecName: Full=DNA replication licensing factor MCM4;
EC=3.6.4.12;
AltName: Full=Cell division control protein 54;
Name=MCM4; Synonyms=CDC54, HCD21; OrderedLocusNames=YPR019W;
ORFNames=YP9531.13;
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].
Dalton S.;
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
COMPLEX, AND MUTAGENESIS OF LYS-574.
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-56, 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).
[5]
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).
[6]
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).
[7]
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 571-646.
PubMed=1454522; DOI=10.1093/nar/20.21.5571;
Coxon A., Maundrell K., Kearsey S.E.;
"Fission yeast cdc21+ belongs to a family of proteins involved in an
early step of chromosome replication.";
Nucleic Acids Res. 20:5571-5577(1992).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-69, 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
S phase execution. {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. {ECO:0000269|PubMed:19896182,
ECO:0000269|PubMed:19910535}.
-!- INTERACTION:
P32354:MCM10; NbExp=3; IntAct=EBI-4326, EBI-5965;
P29469:MCM2; NbExp=15; IntAct=EBI-4326, EBI-10533;
P53091:MCM6; NbExp=7; IntAct=EBI-4326, EBI-10556;
P38132:MCM7; NbExp=3; IntAct=EBI-4326, EBI-4300;
Q12488:PSF1; NbExp=5; IntAct=EBI-4326, EBI-22066;
Q12306:SMT3; NbExp=2; IntAct=EBI-4326, EBI-17490;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- MISCELLANEOUS: Present with 8800 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; U14731; AAA86310.1; -; Genomic_DNA.
EMBL; Z49919; CAA90164.1; -; Genomic_DNA.
EMBL; Z71255; CAA95015.1; -; Genomic_DNA.
EMBL; Z15032; CAA78750.1; -; Genomic_DNA.
EMBL; BK006949; DAA11445.1; -; Genomic_DNA.
PIR; S56050; S56050.
RefSeq; NP_015344.1; NM_001184116.1.
PDB; 3JA8; EM; 3.80 A; 4=1-933.
PDB; 3JC5; EM; 4.70 A; 4=1-933.
PDB; 3JC6; EM; 3.70 A; 4=1-933.
PDB; 3JC7; EM; 4.80 A; 4=1-933.
PDB; 5BK4; EM; 3.90 A; 4/C=1-933.
PDB; 5H7I; EM; 7.10 A; 4=1-933.
PDB; 5U8S; EM; 6.10 A; 4=1-933.
PDB; 5U8T; EM; 4.90 A; 4=1-933.
PDB; 5UDB; EM; 3.90 A; 4=1-933.
PDB; 5V8F; EM; 3.90 A; 4=1-933.
PDB; 5XF8; EM; 7.10 A; 4=1-933.
PDB; 6EYC; EM; 3.80 A; 4=1-933.
PDB; 6F0L; EM; 4.77 A; 4/C=1-933.
PDBsum; 3JA8; -.
PDBsum; 3JC5; -.
PDBsum; 3JC6; -.
PDBsum; 3JC7; -.
PDBsum; 5BK4; -.
PDBsum; 5H7I; -.
PDBsum; 5U8S; -.
PDBsum; 5U8T; -.
PDBsum; 5UDB; -.
PDBsum; 5V8F; -.
PDBsum; 5XF8; -.
PDBsum; 6EYC; -.
PDBsum; 6F0L; -.
ProteinModelPortal; P30665; -.
SMR; P30665; -.
BioGrid; 36196; 142.
ComplexPortal; CPX-2944; MCM complex.
DIP; DIP-2409N; -.
IntAct; P30665; 35.
MINT; P30665; -.
STRING; 4932.YPR019W; -.
iPTMnet; P30665; -.
MaxQB; P30665; -.
PaxDb; P30665; -.
PRIDE; P30665; -.
EnsemblFungi; YPR019W; YPR019W; YPR019W.
GeneID; 856130; -.
KEGG; sce:YPR019W; -.
EuPathDB; FungiDB:YPR019W; -.
SGD; S000006223; MCM4.
GeneTree; ENSGT00910000144163; -.
InParanoid; P30665; -.
KO; K02212; -.
OMA; KNTIRIC; -.
OrthoDB; EOG092C0VUM; -.
BioCyc; YEAST:G3O-34179-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:P30665; -.
Proteomes; UP000002311; Chromosome XVI.
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:0043596; C:nuclear replication fork; 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:0003697; F:single-stranded DNA binding; IMP:SGD.
GO; GO:0006270; P:DNA replication initiation; IGI: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; IPR031327; MCM.
InterPro; IPR008047; MCM_4.
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:SF66; PTHR11630:SF66; 1.
Pfam; PF00493; MCM; 1.
Pfam; PF14551; MCM_N; 1.
Pfam; PF17207; MCM_OB; 1.
PRINTS; PR01657; MCMFAMILY.
PRINTS; PR01660; MCMPROTEIN4.
SMART; SM00350; MCM; 1.
SUPFAM; SSF50249; SSF50249; 1.
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 1 933 DNA replication licensing factor MCM4.
/FTId=PRO_0000194105.
DOMAIN 518 725 MCM.
NP_BIND 568 575 ATP. {ECO:0000255}.
MOTIF 700 703 Arginine finger.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 574 574 K->A: Loss of MCM2-7 complex helicase
activity. {ECO:0000269|PubMed:18657510}.
SEQUENCE 933 AA; 105003 MW; 382D542AE38975E3 CRC64;
MSQQSSSPTK EDNNSSSPVV PNPDSVPPQL SSPALFYSSS SSQGDIYGRN NSQNLSQGEG
NIRAAIGSSP LNFPSSSQRQ NSDVFQSQGR QGRIRSSASA SGRSRYHSDL RSDRALPTSS
SSLGRNGQNR VHMRRNDIHT SDLSSPRRIV DFDTRSGVNT LDTSSSSAPP SEASEPLRII
WGTNVSIQEC TTNFRNFLMS FKYKFRKILD EREEFINNTT DEELYYIKQL NEMRELGTSN
LNLDARNLLA YKQTEDLYHQ LLNYPQEVIS IMDQTIKDCM VSLIVDNNLD YDLDEIETKF
YKVRPYNVGS CKGMRELNPN DIDKLINLKG LVLRSTPVIP DMKVAFFKCN VCDHTMAVEI
DRGVIQEPAR CERIDCNEPN SMSLIHNRCS FADKQVIKLQ ETPDFVPDGQ TPHSISLCVY
DELVDSCRAG DRIEVTGTFR SIPIRANSRQ RVLKSLYKTY VDVVHVKKVS DKRLDVDTST
IEQELMQNKV DHNEVEEVRQ ITDQDLAKIR EVAAREDLYS LLARSIAPSI YELEDVKKGI
LLQLFGGTNK TFTKGGRYRG DINILLCGDP STSKSQILQY VHKITPRGVY TSGKGSSAVG
LTAYITRDVD TKQLVLESGA LVLSDGGVCC IDEFDKMSDS TRSVLHEVME QQTISIAKAG
IITTLNARSS ILASANPIGS RYNPNLPVTE NIDLPPPLLS RFDLVYLVLD KVDEKNDREL
AKHLTNLYLE DKPEHISQDD VLPVEFLTMY ISYAKEHIHP IITEAAKTEL VRAYVGMRKM
GDDSRSDEKR ITATTRQLES MIRLAEAHAK MKLKNVVELE DVQEAVRLIR SAIKDYATDP
KTGKIDMNLV QTGKSVIQRK LQEDLSREIM NVLKDQASDS MSFNELIKQI NEHSQDRVES
SDIQEALSRL QQEDKVIVLG EGVRRSVRLN NRV


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