MCM2_XENTR
ID MCM2_XENTR Reviewed; 884 AA.
AC Q6DIH3;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DNA replication licensing factor mcm2;
DE AltName: Full=Minichromosome maintenance protein 2;
GN Name=mcm2 {ECO:0000312|EMBL:AAH75567.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH75567.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the putative replicative helicase essential for 'once per cell
CC cycle' DNA replication initiation and elongation in eukaryotic cells.
CC The active ATPase sites in the MCM2-7 ring are formed through the
CC interaction surfaces of two neighboring subunits such that a critical
CC structure of a conserved arginine finger motif is provided in trans
CC relative to the ATP-binding site of the Walker A box of the adjacent
CC subunit. The six ATPase active sites, however, are likely to contribute
CC differentially to the complex helicase activity.
CC {ECO:0000250|UniProtKB:P49736}.
CC -!- SUBUNIT: Component of the mcm2-7 complex (RLF-M). The complex forms a
CC toroidal hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-
CC mcm7-mcm3-mcm5 (By similarity). Component of the replisome complex (By
CC similarity). Component of the CMG helicase complex, composed of the
CC mcm2-7 complex, the GINS complex and cdc45 (By similarity).
CC {ECO:0000250|UniProtKB:P49736, ECO:0000250|UniProtKB:P55861}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55861}.
CC Chromosome {ECO:0000250|UniProtKB:P55861}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:P55861}.
CC -!- PTM: May be in a phosphorylated state in the mitotic mcm complex.
CC Phosphorylated in the interphase mcm complex. Phosphorylated by the
CC cdc7-dbf4 and cdc7-dbf4b complexes (By similarity).
CC {ECO:0000250|UniProtKB:P49736}.
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. Specifically a MCM467 subcomplex is shown to
CC have in vitro helicase activity which is inhibited by the MCM2 subunit.
CC The MCM2-7 hexamer is the proposed physiological active complex.
CC {ECO:0000250|UniProtKB:P49736}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR EMBL; BC075567; AAH75567.1; -; mRNA.
DR RefSeq; NP_001006772.1; NM_001006771.1.
DR AlphaFoldDB; Q6DIH3; -.
DR SMR; Q6DIH3; -.
DR STRING; 8364.ENSXETP00000060521; -.
DR PaxDb; Q6DIH3; -.
DR GeneID; 448458; -.
DR KEGG; xtr:448458; -.
DR CTD; 4171; -.
DR Xenbase; XB-GENE-999974; mcm2.
DR eggNOG; KOG0477; Eukaryota.
DR InParanoid; Q6DIH3; -.
DR OrthoDB; 266497at2759; -.
DR Reactome; R-XTR-176187; Activation of ATR in response to replication stress.
DR Reactome; R-XTR-68867; Assembly of the pre-replicative complex.
DR Reactome; R-XTR-68962; Activation of the pre-replicative complex.
DR Reactome; R-XTR-69052; Switching of origins to a post-replicative state.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000002059; Expressed in ovary and 17 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISS:UniProtKB.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR GO; GO:1905775; P:negative regulation of DNA helicase activity; IEA:InterPro.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; ISS:UniProtKB.
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 PANTHER; PTHR11630:SF44; PTHR11630:SF44; 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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Chromosome; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..884
FT /note="DNA replication licensing factor mcm2"
FT /id="PRO_0000239939"
FT DOMAIN 458..664
FT /note="MCM"
FT ZN_FING 314..340
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 640..643
FT /note="Arginine finger"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 508..515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 884 AA; 100116 MW; 5C745595329F518E CRC64;
MADSSESFNI ATSPRTGSRR DALTSSPGRD LPPFEDESEG MFGDEVPREE EEDGEELIGD
AMERDYRAIS ELDRYEAEGL DDEDDVEDLT ASQRDAAEQA MRMRDREMGH ELGRMRRGLL
YDSDEEDEDR PARKRRMAER AAEGAPEEDE EMIESIENLE DMKGHTVREW VSMAATRLEI
YHRFKNFLRT HVDEHGHNVF KEKISDMCKE NKESLVVNYE DLAAREHVLA YFLPEAPAEM
LKIFDEAAKE VVLVMYPKYD RIAREIHVRI SHLPLVEELR SLRQLHLNQL IRTSGVVTCC
TGVLPQLSMV KYNCNKCNFI LGPFFQSQNQ EVKPGSCPEC QSLGPFEINM EETVYQNYQR
ITIQESPGKV AAGRLPRSKD AILLADLVDS CKPGDEIELT GTYHNNYDGS LNTANGFPVF
ATVILANHIT KKDDKVAVGE LTDEDVKAIV ALSKDERIGE RIFASIAPSI YGHEDIKRGL
ALALFGGEAK NPGGKHKVRG DINVLLCGDP GTAKSQFLKY VEKVASRAVF TTGQGASAVG
LTAYVQRHPV TKEWTLEAGA LVLADRGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG
IVTSLQARCT IIAASNPIGG RYDPSLTFSE NVDLTEPIVS RFDILCVVRD TVDPVQDEML
ARFVVGSHIK HHPSSKDIAN GEEFALPNTF GVEPLPQEVL KKYIMYSKEK IHPKLNQMDQ
DKVAKMYSDL RKESMATGSI PITVRHIESM IRMAEAHARM HLRDYVVEDD VNMAIRVMLE
SFIDTQKFSV MRSMRKTFAR YLAFRRDNNE LLLFVLKQLV AEQTSYQRNR YGAQQDTIEV
PEKDLVDKAR QINIHNLSAF YDSDLFKMNR FTHDVKKKMI IQQF
