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Database: UniProt
Entry: MCM3_ARATH
LinkDB: MCM3_ARATH
Original site: MCM3_ARATH 
ID   MCM3_ARATH              Reviewed;         776 AA.
AC   Q9FL33; O65400;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=DNA replication licensing factor MCM3;
DE            EC=3.6.4.12;
DE   AltName: Full=Minichromosome maintenance protein 3;
DE            Short=AtMCM3;
GN   Name=MCM3; OrderedLocusNames=At5g46280; ORFNames=MPL12.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RA   Dodeman V.L., Phan T., Sabelli P., Bergounioux C.;
RT   "Expression analysis of Arabidopsis thaliana MCM3 homolog during the cell
RT   cycle.";
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12089153; DOI=10.1074/jbc.m205125200;
RA   Stevens R., Mariconti L., Rossignol P., Perennes C., Cella R.,
RA   Bergounioux C.;
RT   "Two E2F sites in the Arabidopsis MCM3 promoter have different roles in
RT   cell cycle activation and meristematic expression.";
RL   J. Biol. Chem. 277:32978-32984(2002).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=17556508; DOI=10.1104/pp.107.101105;
RA   Shultz R.W., Tatineni V.M., Hanley-Bowdoin L., Thompson W.F.;
RT   "Genome-wide analysis of the core DNA replication machinery in the higher
RT   plants Arabidopsis and rice.";
RL   Plant Physiol. 144:1697-1714(2007).
RN   [6]
RP   SUBUNIT, AND INTERACTION WITH ETG1.
RX   PubMed=18528439; DOI=10.1038/emboj.2008.107;
RA   Takahashi N., Lammens T., Boudolf V., Maes S., Yoshizumi T., De Jaeger G.,
RA   Witters E., Inze D., De Veylder L.;
RT   "The DNA replication checkpoint aids survival of plants deficient in the
RT   novel replisome factor ETG1.";
RL   EMBO J. 27:1840-1851(2008).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=19357199; DOI=10.1104/pp.109.136614;
RA   Shultz R.W., Lee T.J., Allen G.C., Thompson W.F., Hanley-Bowdoin L.;
RT   "Dynamic localization of the DNA replication proteins MCM5 and MCM7 in
RT   plants.";
RL   Plant Physiol. 150:658-669(2009).
CC   -!- FUNCTION: Probable component of the MCM2-7 complex (MCM complex) that
CC       may function as a DNA helicase and which is essential to undergo a
CC       single round of replication initiation and elongation per cell cycle in
CC       eukaryotic cells. {ECO:0000269|PubMed:12089153}.
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 minichromosome maintenance (MCM) complex, a
CC       heterotetramer composed of MCM2, MCM3, MCM4, MCM5, MCM6 and MCM7.
CC       Interacts with ETG1. {ECO:0000269|PubMed:18528439}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in root meristem, shoot apex and flower
CC       buds. {ECO:0000269|PubMed:12089153, ECO:0000269|PubMed:19357199}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR   EMBL; AJ000058; CAA03887.1; -; mRNA.
DR   EMBL; AB010698; BAB11083.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95362.1; -; Genomic_DNA.
DR   PIR; T52118; T52118.
DR   RefSeq; NP_199440.1; NM_123997.3.
DR   AlphaFoldDB; Q9FL33; -.
DR   SMR; Q9FL33; -.
DR   BioGRID; 19919; 13.
DR   IntAct; Q9FL33; 1.
DR   MINT; Q9FL33; -.
DR   STRING; 3702.Q9FL33; -.
DR   iPTMnet; Q9FL33; -.
DR   PaxDb; 3702-AT5G46280-1; -.
DR   ProteomicsDB; 238240; -.
DR   EnsemblPlants; AT5G46280.1; AT5G46280.1; AT5G46280.
DR   GeneID; 834670; -.
DR   Gramene; AT5G46280.1; AT5G46280.1; AT5G46280.
DR   KEGG; ath:AT5G46280; -.
DR   Araport; AT5G46280; -.
DR   TAIR; AT5G46280; MCM3.
DR   eggNOG; KOG0479; Eukaryota.
DR   HOGENOM; CLU_000995_6_0_1; -.
DR   InParanoid; Q9FL33; -.
DR   OrthoDB; 147095at2759; -.
DR   PhylomeDB; Q9FL33; -.
DR   BRENDA; 3.6.4.12; 399.
DR   PRO; PR:Q9FL33; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FL33; baseline and differential.
DR   Genevisible; Q9FL33; AT.
DR   GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR   GO; GO:0000347; C:THO complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; TAS:TAIR.
DR   CDD; cd17754; MCM3; 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; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008046; Mcm3.
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:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 1.
DR   Pfam; PF00493; MCM; 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; PR01659; MCMPROTEIN3.
DR   SMART; SM00382; AAA; 1.
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   ATP-binding; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..776
FT                   /note="DNA replication licensing factor MCM3"
FT                   /id="PRO_0000194097"
FT   DOMAIN          285..491
FT                   /note="MCM"
FT   REGION          643..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           467..470
FT                   /note="Arginine finger"
FT   COMPBIAS        643..677
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         335..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        502
FT                   /note="G -> S (in Ref. 1; CAA03887)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   776 AA;  86357 MW;  48EB068DC2AA8894 CRC64;
     MDVPEETRLR HKRDFIQFLD SMYMEEIKAL VHQKRHRLII NISDIHHHFR EVASRILKNP
     NEYMQSFCDA ATEATRAIDP KYLKEGELVL VGFEGYFVSR VVTPRELLSD FIGSMVCVEG
     IVTKCSLVRP KVVKSVHFCP STGEFTNRDY RDITSHAGLP TGSVYPTRDD KGNLLVTEYG
     LCKYKDHQTL SIQEVPENAA PGQLPRSVDV IAEDDLVDSC KPGDRVSVFG IYKALPGKSK
     GSVNGVFRTI LIANNIALLN KEANAPIYTK QDLDNIKNIA RRDDAFDLLA RSLAPSIYGH
     AWIKKAVVLL MLGGVEKNLK NGTHLRGDIN MMMVGDPSVA KSQLLRAIMN IAPLAISTTG
     RGSSGVGLTA AVTSDQETGE RRLEAGAMVL ADKGIVCIDE FDKMNDQDRV AIHEVMEQQT
     VTIAKAGIHA SLNARCSVVA AANPIYGTYD RSLTPTKNIG LPDSLLSRFD LLFIVLDQMD
     AGIDSMISEH VLRMHRYKND RGEAGPDGSL PYAREDNAES EMFVKYNQTL HGKKKRGQTH
     DKTLTIKFLK KYIHYAKHRI TPKLTDEASE RIAEAYADLR NAGSDTKTGG TLPITARTLE
     TIIRLATAHA KMKLSSEVTK ADAEAALKLM NFAIYHQELT EMDDREQEER QREQAEQERT
     PSGRRGNQRR NNEDGAENDT ANVDSETADP MEVDEPSVEQ FSGTVSAARI ETFERVFGQH
     MRTHRLDDIS IADIETVVNN NGVGASRYSA DEIMALLEKL QDDNKVMISD GKVHII
//
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