ID D3Z2K9_MOUSE Unreviewed; 142 AA. AC D3Z2K9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 25-APR-2018, entry version 65. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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) CC which is the putative replicative helicase essential for 'once per CC cell cycle' DNA replication initiation and elongation in CC eukaryotic cells. The active ATPase sites in the mcm2-7 ring are CC formed through the interaction surfaces of two neighboring CC subunits such that a critical structure of a conserved arginine CC finger motif is provided in trans relative to the ATP-binding site CC of the Walker A box of the adjacent subunit. The six ATPase active CC sites, however, are likely to contribute differentially to the CC complex helicase activity. {ECO:0000256|RuleBase:RU365012}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|RuleBase:RU365012}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365012}. CC -!- SIMILARITY: Belongs to the MCM family. CC {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 Ensembl; ENSMUST00000153867; ENSMUSP00000121566; ENSMUSG00000029730. DR MGI; MGI:1298398; Mcm7. DR eggNOG; KOG0482; Eukaryota. DR eggNOG; COG1241; LUCA. DR GeneTree; ENSGT00900000141136; -. DR HOGENOM; HOG000213574; -. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000029730; -. 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:0003678; F:DNA helicase activity; IEA:Ensembl. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:Ensembl. 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 Complete proteome {ECO:0000313|Proteomes:UP000000589}; 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 42 141 MCM_OB. {ECO:0000259|Pfam:PF17207}. FT NON_TER 142 142 {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 //