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DNA replication licensing factor MCM3 (EC 3.6.4.12) (Minichromosome maintenance protein 3)

 MCM3_YEAST              Reviewed;         971 AA.
P24279; D3DLL7;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
10-OCT-2018, entry version 186.
RecName: Full=DNA replication licensing factor MCM3;
EC=3.6.4.12;
AltName: Full=Minichromosome maintenance protein 3;
Name=MCM3; OrderedLocusNames=YEL032W; ORFNames=SYGP-ORF23;
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=2233713; DOI=10.1128/MCB.10.11.5707;
Gibson S.T., Suroski R.T., Tye B.K.;
"The phenotype of the minichromosome maintenance mutant mcm3 is
characteristic of mutants defective in DNA replication.";
Mol. Cell. Biol. 10:5707-5720(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-868, 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777 AND SER-781, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[5]
RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
COMPLEX, AND MUTAGENESIS OF LYS-415.
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).
[6]
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).
[7]
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).
[8]
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).
[9]
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).
[10]
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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-761 AND SER-781, 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. Necessary
for cell growth. {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. {ECO:0000269|PubMed:15023545,
ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535}.
-!- INTERACTION:
P25651:CSM1; NbExp=2; IntAct=EBI-10541, EBI-22001;
P29496:MCM5; NbExp=5; IntAct=EBI-10541, EBI-10549;
P38132:MCM7; NbExp=2; IntAct=EBI-10541, EBI-4300;
Q12306:SMT3; NbExp=2; IntAct=EBI-10541, EBI-17490;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 35100 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. The MCM2-7 hexamer is the
proposed physiological active complex.
-!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X53540; CAA37616.1; -; Genomic_DNA.
EMBL; U18779; AAB65010.1; -; Genomic_DNA.
EMBL; BK006939; DAA07621.1; -; Genomic_DNA.
PIR; A36376; A36376.
RefSeq; NP_010882.1; NM_001178847.1.
PDB; 3JA8; EM; 3.80 A; 3=1-971.
PDB; 3JC5; EM; 4.70 A; 3=1-971.
PDB; 3JC6; EM; 3.70 A; 3=1-971.
PDB; 3JC7; EM; 4.80 A; 3=1-971.
PDB; 5BK4; EM; 3.90 A; 3/B=1-971.
PDB; 5H7I; EM; 7.10 A; 3=1-971.
PDB; 5U8S; EM; 6.10 A; 3=1-971.
PDB; 5U8T; EM; 4.90 A; 3=1-971.
PDB; 5UDB; EM; 3.90 A; 3=1-971.
PDB; 5V8F; EM; 3.90 A; 3=1-971.
PDB; 5XF8; EM; 7.10 A; 3=1-971.
PDB; 6EYC; EM; 3.80 A; 3=1-971.
PDB; 6F0L; EM; 4.77 A; 3/B=1-971.
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; P24279; -.
SMR; P24279; -.
BioGrid; 36697; 396.
ComplexPortal; CPX-2944; MCM complex.
DIP; DIP-2407N; -.
IntAct; P24279; 35.
MINT; P24279; -.
STRING; 4932.YEL032W; -.
iPTMnet; P24279; -.
MaxQB; P24279; -.
PaxDb; P24279; -.
PRIDE; P24279; -.
EnsemblFungi; YEL032W; YEL032W; YEL032W.
GeneID; 856680; -.
KEGG; sce:YEL032W; -.
EuPathDB; FungiDB:YEL032W; -.
SGD; S000000758; MCM3.
GeneTree; ENSGT00900000141082; -.
HOGENOM; HOG000224126; -.
InParanoid; P24279; -.
KO; K02541; -.
OMA; RNDQNTK; -.
OrthoDB; EOG092C0VUM; -.
BioCyc; YEAST:G3O-30154-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:P24279; -.
Proteomes; UP000002311; Chromosome V.
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; IPI:SGD.
GO; GO:0042555; C:MCM 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:0003682; F:chromatin binding; IDA:SGD.
GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:1904931; F:MCM complex binding; 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:0032508; P:DNA duplex unwinding; IEA:GOC.
GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD.
GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
GO; GO:1902975; P:mitotic DNA replication initiation; 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; IPR008046; Mcm3.
InterPro; IPR018525; MCM_CS.
InterPro; IPR001208; MCM_dom.
InterPro; IPR033762; MCM_OB.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11630; PTHR11630; 1.
Pfam; PF00493; MCM; 1.
Pfam; PF17207; MCM_OB; 1.
PRINTS; PR01657; MCMFAMILY.
PRINTS; PR01659; MCMPROTEIN3.
SMART; SM00382; AAA; 1.
SMART; SM00350; MCM; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00847; MCM_1; 1.
PROSITE; PS50051; MCM_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; DNA replication;
DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 971 DNA replication licensing factor MCM3.
/FTId=PRO_0000194099.
DOMAIN 359 566 MCM.
NP_BIND 409 416 ATP. {ECO:0000255}.
MOTIF 541 544 Arginine finger.
MOD_RES 761 761 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 777 777 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:19779198}.
MOD_RES 868 868 Phosphothreonine.
{ECO:0000244|PubMed:17330950}.
MUTAGEN 415 415 K->A: No effect on MCM2-7 complex
helicase activity. Loss of MCM2-7 complex
helicase activity; when associated with
MCM5 A-422. Reduces MCM2-7 complex
helicase activity; when associated with
MCM2 A-549.
{ECO:0000269|PubMed:18657510}.
SEQUENCE 971 AA; 107518 MW; 43DD4DACAF4456DC CRC64;
MEGSTGFDGD ATTFFAPDAV FGDRVRRFQE FLDTFTSYRD SVRSIQVYNS NNAANYNDDQ
DDADERDLLG DDDGDDLEKE KKAASSTSLN ILPHRIIISL DDLREFDRSF WSGILVEPAY
FIPPAEKALT DLADSMDDVP HPNASAVSSR HPWKLSFKGS FGAHALSPRT LTAQHLNKLV
SVEGIVTKTS LVRPKLIRSV HYAAKTGRFH YRDYTDATTT LTTRIPTPAI YPTEDTEGNK
LTTEYGYSTF IDHQRITVQE MPEMAPAGQL PRSIDVILDD DLVDKTKPGD RVNVVGVFKS
LGAGGMNQSN SNTLIGFKTL ILGNTVYPLH ARSTGVAARQ MLTDFDIRNI NKLSKKKDIF
DILSQSLAPS IYGHDHIKKA ILLMLMGGVE KNLENGSHLR GDINILMVGD PSTAKSQLLR
FVLNTASLAI ATTGRGSSGV GLTAAVTTDR ETGERRLEAG AMVLADRGVV CIDEFDKMTD
VDRVAIHEVM EQQTVTIAKA GIHTTLNARC SVIAAANPVF GQYDVNRDPH QNIALPDSLL
SRFDLLFVVT DDINEIRDRS ISEHVLRTHR YLPPGYLEGE PVRERLNLSL AVGEDADINP
EEHSNSGAGV ENEGEDDEDH VFEKFNPLLQ AGAKLAKNKG NYNGTEIPKL VTIPFLRKYV
QYAKERVIPQ LTQEAINVIV KNYTDLRNDD NTKKSPITAR TLETLIRLAT AHAKVRLSKT
VNKVDAKVAA NLLRFALLGE DIGNDIDEEE SEYEEALSKR SPQKSPKKRQ RVRQPASNSG
SPIKSTPRRS TASSVNATPS SARRILRFQD DEQNAGEDDN DIMSPLPADE EAELQRRLQL
GLRVSPRRRE HLHAPEEGSS GPLTEVGTPR LPNVSSAGQD DEQQQSVISF DNVEPGTIST
GRLSLISGII ARLMQTEIFE EESYPVASLF ERINEELPEE EKFSAQEYLA GLKIMSDRNN
LMVADDKVWR V


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