ID A0A096W1R4_9LECA Unreviewed; 163 AA. AC A0A096W1R4; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 11-DEC-2019, entry version 19. 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}; OS Cetraria kamtczatica. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes; OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Parmeliaceae; OC Cetraria. OX NCBI_TaxID=513565 {ECO:0000313|EMBL:AGZ15608.1}; RN [1] {ECO:0000313|EMBL:AGZ15608.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CKA 01 {ECO:0000313|EMBL:AGZ15608.1}; RX PubMed=25480713; DOI=10.3732/ajb.1400439; RA Saag L., Mark K., Saag A., Randlane T.; RT "Species delimitation in the lichenized fungal genus Vulpicida RT (Parmeliaceae, Ascomycota) using gene concatenation and coalescent-based RT species tree approaches."; RL Am. J. Bot. 101:2169-2182(2014). 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; KC990163; AGZ15608.1; -; Genomic_DNA. 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; 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 PRINTS; PR01663; MCMPROTEIN7. 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 136..163 FT /note="MCM" FT /evidence="ECO:0000259|PROSITE:PS50051" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AGZ15608.1" FT NON_TER 163 FT /evidence="ECO:0000313|EMBL:AGZ15608.1" SQ SEQUENCE 163 AA; 18546 MW; ED6A633A0CE6A48F CRC64; SKQFTPMTEC PSDECKQNNS KGQLFLSTRA SKFLPFQEVK IQEMADQVPV GHIPRTLTVH CHGTLTRQIN PGDVIDVAGI FLPTPYTGFK AIRAGLLTDT YLEAQHVNQH KKAYDDLVFD AKTFRRIEQY KHSGHMYEYL SRSIAPEIYG HQDVKKALLL LLI //