ID D3Z2K9_MOUSE Unreviewed; 142 AA. AC D3Z2K9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-OCT-2020, entry version 83. DE RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012}; DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012}; DE Flags: Fragment; GN Name=Mcm7 {ECO:0000313|Ensembl:ENSMUSP00000121566, GN ECO:0000313|MGI:MGI:1298398}; GN Synonyms=MCM7 {ECO:0000256|RuleBase:RU365012}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000121566, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000121566, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121566, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000121566} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121566}; RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. 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:0000256|RuleBase:RU365012}. 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 ECO:0000256|RuleBase:RU365012}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|RuleBase:RU365012}. CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU365012}. 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 EMBL; AC151719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; D3Z2K9; -. DR MaxQB; D3Z2K9; -. DR Antibodypedia; 1289; 1114 antibodies. DR Ensembl; ENSMUST00000153867; ENSMUSP00000121566; ENSMUSG00000029730. DR MGI; MGI:1298398; Mcm7. DR GeneTree; ENSGT01000000214610; -. DR HOGENOM; CLU_126876_0_0_1; -. DR OMA; NAYTCDR; -. DR ChiTaRS; Mcm7; mouse. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000029730; Expressed in epiblast (generic) and 153 other tissues. 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:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro. DR InterPro; IPR031327; MCM. DR InterPro; IPR008050; MCM7. DR InterPro; IPR033762; MCM_OB. DR InterPro; IPR012340; NA-bd_OB-fold. DR PANTHER; PTHR11630; PTHR11630; 1. DR PANTHER; PTHR11630:SF26; PTHR11630:SF26; 1. DR Pfam; PF17207; MCM_OB; 1. DR PRINTS; PR01663; MCMPROTEIN7. DR SUPFAM; SSF50249; SSF50249; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|RuleBase:RU365012}; KW Cell cycle {ECO:0000256|RuleBase:RU365012}; KW DNA replication {ECO:0000256|RuleBase:RU365012}; KW DNA-binding {ECO:0000256|RuleBase:RU365012}; KW Helicase {ECO:0000256|RuleBase:RU365012}; KW Hydrolase {ECO:0000256|RuleBase:RU365012}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU365012}; KW Nucleus {ECO:0000256|RuleBase:RU365012}; KW Proteomics identification {ECO:0000213|EPD:D3Z2K9, KW ECO:0000213|MaxQB:D3Z2K9, ECO:0000213|PeptideAtlas:D3Z2K9}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT DOMAIN 42..142 FT /note="MCM_OB" FT /evidence="ECO:0000259|Pfam:PF17207" FT NON_TER 142 FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000121566" SQ SEQUENCE 142 AA; 16246 MW; ED01ECAEBBAA0A9A CRC64; MMEQRSRDPG AVRNPQNQYP SELMRRFELY FRGPSSSKPR VIREVRADSV GKLLTVRGIV TRVSEVKPRM VVATYTCDQC GAETYQPIQS PTFMPLIMCP SQECQTNRSG GRLYLQTRGS KFVKFQEMKI QEHSDQVPVG NI //