ID   MCM5_CAEEL              Reviewed;         759 AA.
AC   Q21902;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=DNA replication licensing factor mcm-5;
DE            EC=3.6.4.12;
GN   Name=mcm-5; ORFNames=R10E4.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Acts as a 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. Core
CC       component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that
CC       unwinds template DNA during replication, and around which the replisome
CC       is built. The active ATPase sites in the MCM2-7 ring are formed through
CC       the interaction surfaces of two neighboring subunits such that a
CC       critical structure of a conserved arginine finger motif is provided in
CC       trans relative to the ATP-binding site of the Walker A box of the
CC       adjacent subunit. The six ATPase active sites, however, are likely to
CC       contribute differentially to the complex helicase activity.
CC       {ECO:0000250|UniProtKB:P33992}.
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:0000250|UniProtKB:P33992};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:P33992};
CC   -!- SUBUNIT: Component of the mcm2-7 complex. The complex forms a toroidal
CC       hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-mcm7-
CC       mcm3-mcm5 (By simililarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P33992}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:P33992}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR   EMBL; Z50874; CAA90765.1; -; Genomic_DNA.
DR   PIR; T24130; T24130.
DR   RefSeq; NP_497858.1; NM_065457.4.
DR   PDB; 8OUW; EM; 3.75 A; 5=1-759.
DR   PDBsum; 8OUW; -.
DR   AlphaFoldDB; Q21902; -.
DR   EMDB; EMD-17204; -.
DR   SMR; Q21902; -.
DR   BioGRID; 40789; 15.
DR   ComplexPortal; CPX-4482; MCM complex.
DR   STRING; 6239.R10E4.4.2; -.
DR   EPD; Q21902; -.
DR   PaxDb; 6239-R10E4-4-1; -.
DR   PeptideAtlas; Q21902; -.
DR   EnsemblMetazoa; R10E4.4.1; R10E4.4.1; WBGene00003157.
DR   GeneID; 175552; -.
DR   KEGG; cel:CELE_R10E4.4; -.
DR   UCSC; R10E4.4.1; c. elegans.
DR   AGR; WB:WBGene00003157; -.
DR   WormBase; R10E4.4; CE03558; WBGene00003157; mcm-5.
DR   eggNOG; KOG0481; Eukaryota.
DR   GeneTree; ENSGT01050000244824; -.
DR   HOGENOM; CLU_000995_7_2_1; -.
DR   InParanoid; Q21902; -.
DR   OMA; ITYCKTR; -.
DR   OrthoDB; 5476523at2759; -.
DR   PhylomeDB; Q21902; -.
DR   Reactome; R-CEL-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR   Reactome; R-CEL-68962; Activation of the pre-replicative complex.
DR   Reactome; R-CEL-69052; Switching of origins to a post-replicative state.
DR   PRO; PR:Q21902; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003157; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR   GO; GO:0006279; P:premeiotic DNA replication; NAS:ComplexPortal.
DR   CDD; cd17756; MCM5; 1.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
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; IPR008048; MCM5.
DR   InterPro; IPR018525; MCM_CS.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR041562; MCM_lid.
DR   InterPro; IPR027925; MCM_N.
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:SF42; DNA REPLICATION LICENSING FACTOR MCM5; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF17855; MCM_lid; 1.
DR   Pfam; PF14551; MCM_N; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   PRINTS; PR01661; MCMPROTEIN5.
DR   SMART; SM00350; MCM; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00847; MCM_1; 1.
DR   PROSITE; PS50051; MCM_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell cycle; Cytoplasm; DNA replication;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..759
FT                   /note="DNA replication licensing factor mcm-5"
FT                   /id="PRO_0000194110"
FT   DOMAIN          330..536
FT                   /note="MCM"
FT   MOTIF           511..514
FT                   /note="Arginine finger"
FT   BINDING         370
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="ligand shared with MCM3"
FT                   /evidence="ECO:0000250|UniProtKB:P33992"
SQ   SEQUENCE   759 AA;  84936 MW;  8D81B2AB5090A92B CRC64;
     MSNLDNPGIY YQERFFANDG VPDTGRELIA EYRQLITQFR NFIRDFSTGG FGMIYRDQLK
     RNYFSHEYRL EINLNHLKNF DEDIEMKLRK FPGKVLPALE EAAKIVADEI TTPRPKGEEK
     LHDIQVTLTL DEYPTSLRQV KSAQVSQVVK ISGIIVAAAQ VRSKATKVTL QCRQCKHTIP
     DVSIKPGLEG FALPRTCAAP QQGQMQRCPI DPYIMLPDKC ECVDYQTLKL QENPEDVPHG
     EMPRHLQLFT ERYLTDKVVP GNRVTIVGVY SIKKLIQKKG GDKSLQGIRT PYLRVLGIHM
     ETSGPGRTNF TTFTPEEERM FKTLAQRKDA YELIAKSIAP SIYGSADIKK SIACLLFGGA
     RKKLPDGITR RGDINVLLLG DPGTAKSQLL KFVEQVSPIG VYTSGKGSSA AGLTASVIRD
     PQSRSFIMEG GAMVLADGGV VCIDEFDKMR EDDRVAIHEA MEQQTISIAK AGITTTLNSR
     CSVLAAANSV YGRWDESRGD DNIDFMPTIL SRFDMIYIVK DTHDVLKDAT LAKHVIEVHV
     NASAAKERDI AGVPKTATTD SDGVMTMFDT DGFLTIEFLK KFVTYARLNC GPRLTPQASE
     KLVNHYVKMR NPVVNADAFK SGKKAHNSAI PITVRQLEAI VRIAESIAKM ELQQFATDKH
     VEEALRLFRV STIEAAATGN LAGVEGFTST ADQEALNRIE VQMKKRFAIG THVSEHLIVQ
     DFVARQHYRE SLVKKVIDNL VRRGDLQQKM QRKMLYRVR
//