ID   MCM2_ORYSI              Reviewed;         961 AA.
AC   B8BKI8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=DNA replication licensing factor MCM2;
DE            EC=3.6.4.12;
DE   AltName: Full=Minichromosome maintenance protein 2;
GN   ORFNames=OsI_36121;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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:0000250}.
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       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR   EMBL; CM000136; EEC68174.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8BKI8; -.
DR   SMR; B8BKI8; -.
DR   STRING; 39946.B8BKI8; -.
DR   PRIDE; B8BKI8; -.
DR   EnsemblPlants; BGIOSGA035270-TA; BGIOSGA035270-PA; BGIOSGA035270.
DR   Gramene; BGIOSGA035270-TA; BGIOSGA035270-PA; BGIOSGA035270.
DR   HOGENOM; CLU_000995_0_1_1; -.
DR   OMA; DCVKCGY; -.
DR   Proteomes; UP000007015; Chromosome 11.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblPlants.
DR   GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR   GO; GO:0000347; C:THO complex; IEA:EnsemblPlants.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; 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; IEA:EnsemblPlants.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR   GO; GO:1905775; P:negative regulation of DNA helicase activity; IEA:InterPro.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:EnsemblPlants.
DR   GO; GO:0010082; P:regulation of root meristem growth; IEA:EnsemblPlants.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008045; MCM2.
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; PTHR11630; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF12619; MCM2_N; 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; PR01658; MCMPROTEIN2.
DR   SMART; SM00350; MCM; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00847; MCM_1; 1.
DR   PROSITE; PS50051; MCM_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW   Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..961
FT                   /note="DNA replication licensing factor MCM2"
FT                   /id="PRO_0000425988"
FT   DOMAIN          524..730
FT                   /note="MCM"
FT   ZN_FING         380..406
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           706..709
FT                   /note="Arginine finger"
FT   COMPBIAS        1..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..79
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..220
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         574..581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   961 AA;  108839 MW;  CD67F8128CE839FB CRC64;
     MDDSENNAPS TPGSPGFSTD RLPPNTTTSR GATDPSSYSD DDDDDVVGAE EAEVDPNVLP
     EDDGVVAAEE EEDGEDLFND NYLDDYRRMD EQDQYESVGL DDSIEDERNL DEIMADRRAA
     EAELDARDVR TGAAPDRKLP RMLHDQDTDE DMSFRRPKRH RANFRPPREP RTPRSDDDGD
     GATPSSPGRS QRGMYSGGDV PMTDQTDDDP YEDEFDEEDE MNMYRVQGTL REWVTRDEVR
     RFIAKKFKEF LLTYVNPKNE QGEFEYVRLI NEMVLANKCS LEIDYKQFIY IHPNIAIWLA
     DAPQSVIEVM EEVAKNVVFD LHKNYRNIHQ KIYVRITNLP VYDQIRNIRQ IHLNTMIRIG
     GVVTRRSGVF PQLQQVKYDC SKCGTVLGPF FQNSYTEVKV GSCPECQSKG PFTINVEQTI
     YRNYQKLTLQ ESPGIVPAGR LPRYKEVILL NDLIDCARPG EEIEVTGIYT NNFDLSLNTK
     NGFPVFATVV EANYVAKKQD LFSAYKLTDE DKAEIEKLAK DPRIGERIVK SIAPSIYGHE
     DIKTAIALAM FGGQEKNVKG KHRLRGDINV LLLGDPGTAK SQFLKYVEKT GHRAVYTTGK
     GASAVGLTAA VHKDPVTREW TLEGGALVLA DRGICLIDEF DKMNDQDRVS IHEAMEQQSI
     SISKAGIVTS LQARCSVIAA ANPIGGRYDS SKTFTQNVEL TDPIISRFDV LCVVKDIVDP
     FTDEMLARFV VDSHARSQPK GANLEDRVPT DVEDDPLAAA RQADPDILSQ DMLKKYITYA
     KLNVFPKIHD ADLDKISHVY AELRRESSHG QGVPIAVRHI ESIIRMSEAH ARMHLRSYVS
     QEDVDMAIRV LLDSFISTQK FGVQKALQKN FRKYMTYKKD YNELLLLLLR TLVKDVLHFE
     EIVSGPTTRL THIEVKVEDL KNKAQEYEIY DLRPFFSSAH FRDNNFVLDE GRGIIRHPLA
     A