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Database: UniProt
Entry: A0A0E0MFH2_ORYPU
LinkDB: A0A0E0MFH2_ORYPU
Original site: A0A0E0MFH2_ORYPU 
ID   A0A0E0MFH2_ORYPU        Unreviewed;       873 AA.
AC   A0A0E0MFH2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC11G11490.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC11G11490.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC11G11490.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A0E0MFH2; -.
DR   EnsemblPlants; OPUNC11G11490.1; OPUNC11G11490.1; OPUNC11G11490.
DR   Gramene; OPUNC11G11490.1; OPUNC11G11490.1; OPUNC11G11490.
DR   HOGENOM; CLU_000995_0_1_1; -.
DR   Proteomes; UP000026962; Chromosome 11.
DR   GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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:UniProt.
DR   CDD; cd17753; MCM2; 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; 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; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR   PANTHER; PTHR11630:SF44; DNA REPLICATION LICENSING FACTOR MCM2; 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; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          436..642
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..132
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   873 AA;  99344 MW;  A67112E1E2F9C3B9 CRC64;
     MDEQDQYESV GLDDSIEDER NLDEIMADRR AAEAELDARD VRTGAAPDRK LPRMLHDQDT
     DEDMSFRRPK RHRANFRPPR EPRTPRSDDD GDGATPSSPG RSQRGMYSGG DVPMTDQTDD
     DPYEDEFDEE DEMNMYRVQG TLREWVTRDE VRRFIAKKFK EFLLTYVNPK NEQGEFEYVR
     LINEMVLANK CSLEIDYKQF IYIHPNIAIW LADAPQSVLE VMEEVAKNVV FDLHKNYRNI
     HQKIYVRITN LPVYDQIRNI RQIHLNTMIR IGGVVTRRSG VFPQLQQVKY DCSKCGTILG
     PFFQNSYTEV KVGSCPECQS KGPFTINVEQ TIYRNYQKLT LQESPGIVPA GRLPRYKEVI
     LLNDLIDCAR PGEEIEVTGI YTNNFDLSLN TKNGFPVFAT VVEANYVAKK QDLFSAYKLT
     DEDKAEIEKL AKDPRIGERI VKSIAPSIYG HEDIKTAIAL AMFGGQEKNV KGKHRLRGDI
     NVLLLGDPGT AKSQFLKYVE KTGHRAVYTT GKGASAVGLT AAVHKDPVTR EWTLEGGALV
     LADRGICLID EFDKMNDQDR VSIHEAMEQQ SISISKAGIV TSLQARCSVI AAANPIGGRY
     DSSKTFTQNV ELTDPIISRF DVLCVVKDIV DPFTDEMLAR FVVDSHARSQ PKGANLEDRV
     ATDVEDDPLA AARQADPDIL SQDMLKKYIT YAKLNVFPKI HDADLDKISH VYAELRRESS
     HGQGVPIAVR HIESIIRMSE AHARMHLRSY VSQEDVDMAI RVLLDSFIST QKFGVQKALQ
     KNFRKYMTYK KDYNELLLLL LRTLVKDVLH FEEIVSGPTT RLTHIEVKVE DLKNKAQEYE
     IYDLRPFFSS AHFRDNNFVL DEGRGIIRHP LAA
//
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