ID A0A096W1R4_9LECA Unreviewed; 163 AA. AC A0A096W1R4; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 25-APR-2018, entry version 16. 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; OC Lecanoromycetes; OSLEUM clade; Lecanoromycetidae; Lecanorales; OC Lecanorineae; Parmeliaceae; 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- RT based species tree approaches."; RL Am. J. Bot. 101:2169-2182(2014). 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; 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:InterPro. 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 MCM. {ECO:0000259|PROSITE:PS50051}. FT NON_TER 1 1 {ECO:0000313|EMBL:AGZ15608.1}. FT NON_TER 163 163 {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 //