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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//