ID A0A5B9BRB5_9PEZI Unreviewed; 168 AA. AC A0A5B9BRB5; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 11-DEC-2019, entry version 2. 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:0000256|RuleBase:RU365012, GN ECO:0000313|EMBL:QED90994.1}; OS Seychellomyces sinensis. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Microascales; Microascales incertae sedis; OC Seychellomyces. OX NCBI_TaxID=2604050 {ECO:0000313|EMBL:QED90994.1}; RN [1] {ECO:0000313|EMBL:QED90994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YFM 1.04178 {ECO:0000313|EMBL:QED90994.1}; RA Qiao M., Zheng H., Zhang Z., Yu Z.-F.; RT "Seychellomyces sinensis sp. nov. from China."; RL Mycotaxon 134:391-398(2019). 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|RuleBase:RU365012}; CC -!- SUBCELLULAR LOCATION: Nucleus {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; MK554715; QED90994.1; -; Genomic_DNA. DR InterPro; IPR031327; MCM. DR InterPro; IPR008050; MCM7. DR InterPro; IPR001208; MCM_dom. 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; PF00493; MCM; 1. DR Pfam; PF17207; MCM_OB; 1. DR SMART; SM00350; MCM; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50051; MCM_2; 1. PE 3: Inferred from homology; 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}. FT DOMAIN 115..168 FT /note="MCM" FT /evidence="ECO:0000259|PROSITE:PS50051" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QED90994.1" FT NON_TER 168 FT /evidence="ECO:0000313|EMBL:QED90994.1" SQ SEQUENCE 168 AA; 18575 MW; 98DA584AB1F5737F CRC64; GQLFWSVRAS KFMAFQEVKV QELSDQVPIG QIPRSLTVLC YGSLVRQVNP GDVVDLAGVF LPTPYTGFKA MRAGLLTDTY LEAHYVMQHK KAYSEMLVDY SLTARIDQYR LSGQAYDLLA RSIAPEIYGH VDVKKALLLL LIGGVTKEMG DGMKIRGDIN VCLMGDPG //