MCM5_CAEEL
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 03-AUG-2022, entry version 140.
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 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 (By similarity).
CC {ECO:0000250}.
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 -!- 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 AlphaFoldDB; Q21902; -.
DR SMR; Q21902; -.
DR BioGRID; 40789; 14.
DR ComplexPortal; CPX-4482; MCM complex.
DR STRING; 6239.R10E4.4.1; -.
DR EPD; Q21902; -.
DR PaxDb; Q21902; -.
DR PeptideAtlas; Q21902; -.
DR PRIDE; 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 CTD; 175552; -.
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; 266497at2759; -.
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 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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR11630; 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; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cytoplasm; DNA replication; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; 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 380..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
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
