ID D3Z2K9_MOUSE Unreviewed; 142 AA. AC D3Z2K9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 14-DEC-2022, entry version 93. 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:ENSMUSP00000121566.2, 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:ENSMUSP00000121566.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000121566.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121566.2, 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:ENSMUSP00000121566.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121566.2}; RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which CC is the replicative helicase essential for 'once per cell cycle' DNA CC replication initiation and elongation in eukaryotic cells. The active CC ATPase sites in the MCM2-7 ring are formed through the interaction CC surfaces of two neighboring subunits such that a critical structure of CC a conserved arginine finger motif is provided in trans relative to the CC ATP-binding site of the Walker A box of the adjacent subunit. The six CC ATPase active sites, however, are likely to contribute differentially CC to the complex helicase activity. {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:ARBA00000600}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000256|ARBA:ARBA00000600}; 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 AlphaFoldDB; D3Z2K9; -. DR SMR; D3Z2K9; -. DR MaxQB; D3Z2K9; -. DR ProteomicsDB; 310276; -. DR Antibodypedia; 1289; 1185 antibodies from 44 providers. DR Ensembl; ENSMUST00000153867.8; ENSMUSP00000121566.2; ENSMUSG00000029730.17. DR AGR; MGI:1298398; -. DR MGI; MGI:1298398; Mcm7. DR VEuPathDB; HostDB:ENSMUSG00000029730; -. DR GeneTree; ENSGT01050000244824; -. DR HOGENOM; CLU_126876_0_0_1; -. DR OMA; NAYTCDR; -. DR ChiTaRS; Mcm7; mouse. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000029730; Expressed in ventricular zone and 126 other tissues. DR ExpressionAtlas; D3Z2K9; baseline and differential. 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:0003678; F:DNA helicase activity; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR031327; MCM. DR InterPro; IPR008050; MCM7. DR InterPro; IPR033762; MCM_OB. DR InterPro; IPR012340; NA-bd_OB-fold. DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1. DR PANTHER; PTHR11630:SF26; DNA REPLICATION LICENSING FACTOR MCM7; 1. DR Pfam; PF17207; MCM_OB; 1. DR PRINTS; PR01663; MCMPROTEIN7. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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:0007829|EPD:D3Z2K9, KW ECO:0007829|MaxQB: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:ENSMUSP00000121566.2" SQ SEQUENCE 142 AA; 16246 MW; ED01ECAEBBAA0A9A CRC64; MMEQRSRDPG AVRNPQNQYP SELMRRFELY FRGPSSSKPR VIREVRADSV GKLLTVRGIV TRVSEVKPRM VVATYTCDQC GAETYQPIQS PTFMPLIMCP SQECQTNRSG GRLYLQTRGS KFVKFQEMKI QEHSDQVPVG NI //