ID A0A096W1R4_9LECA Unreviewed; 163 AA. AC A0A096W1R4; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 22-FEB-2023, entry version 26. 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 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|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 AlphaFoldDB; A0A096W1R4; -. DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt. DR GO; GO:0042555; C:MCM complex; IEA:InterPro. DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt. DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt. 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:0006270; P:DNA replication initiation; IEA:InterPro. DR GO; GO:0033260; P:nuclear DNA replication; IEA:UniProt. DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. 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 InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1. DR PANTHER; PTHR11630:SF26; DNA REPLICATION LICENSING FACTOR MCM7; 1. DR Pfam; PF00493; MCM; 1. DR Pfam; PF17207; MCM_OB; 1. DR PRINTS; PR01663; MCMPROTEIN7. DR SMART; SM00350; MCM; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|ARBA:ARBA00023125, 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 //