MCM5B_XENLA
ID MCM5B_XENLA Reviewed; 735 AA.
AC Q6PCI7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=DNA replication licensing factor mcm5-B {ECO:0000305};
DE Short=xMCM5-B;
DE EC=3.6.4.12;
DE AltName: Full=CDC46 homolog B;
DE Short=xCDC46-B;
GN Name=mcm5-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH59310.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH59310.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P55862}.
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 (RLF-M). The complex forms a
CC toroidal hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-
CC mcm7-mcm3-mcm5. The heterodimer of mmcm3/mcm5 interacts with mcm4,
CC mmcm6, mcm7 and weakly with mcm2. Component of the CMG helicase
CC complex, composed of the mcm2-7 complex, the GINS complex and cdc45.
CC {ECO:0000250|UniProtKB:P55862}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55862}.
CC Chromosome {ECO:0000250|UniProtKB:P55862}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:P55862}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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; BC059310; AAH59310.1; -; mRNA.
DR RefSeq; NP_001080009.1; NM_001086540.1.
DR AlphaFoldDB; Q6PCI7; -.
DR SMR; Q6PCI7; -.
DR DNASU; 379699; -.
DR GeneID; 379699; -.
DR KEGG; xla:379699; -.
DR CTD; 379699; -.
DR Xenbase; XB-GENE-985671; mcm5.S.
DR OMA; FLEIDIM; -.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 379699; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISS:UniProtKB.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Chromosome; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..735
FT /note="DNA replication licensing factor mcm5-B"
FT /id="PRO_0000239940"
FT DOMAIN 332..538
FT /note="MCM"
FT /evidence="ECO:0000255"
FT MOTIF 513..516
FT /note="Arginine finger"
FT BINDING 382..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 735 AA; 82505 MW; F9B0745B9D2B0734 CRC64;
MSGFDDLGIY YSDSFGGEQP VGDDGQAKKS QLKKRFREFL RQYRVGTDRT GFTFKYRDEL
KRHYNLGEYW IEVEMEDLAS FDEDLADYLY KQPTEHLQLL EEAAQEVADE VTRPRPAGEE
TIQEIQVMLR SDANPANIRN LKSEQMSHLV KIPGIIIAAT AVRAKATKIS IQCRSCRNTI
GNIAVRPGLE GYAMPRKCNT EQAGRPKCPL DPYFIIPDKC KCVDFQTLKL QESPDAVPHG
ELPRHMQLYC DRYLCDKVVP GNRVTIMGIY SIQKSGKTST KGRDRVGVGI RSSYIRVVGI
QVDTEGTGRS AAGTITPQEE EEFRRLAVKP DIYETVAKSI APSIYGSTDI KKAIACLLFG
GSRKRLPDGL TRRGDVNLLM LGDPGTAKSQ LLKFVERCSP IGVYTSGKGS SAAGLTASVM
RDPVSRNFIM EGGAMVLADG GVVCIDEFDK MREDDRVAIH EAMEQQTISI AKAGITTTLN
SRCSVLAAAN SVYGRWDDTK GEENIDFMPT ILSRFDMIFI VKDEHNEQRD MTLAKHVMNV
HLSARTQSSS VEGEVDLNTL KKFIAYCRAK CGPRLSAEAA EKLKNRYILM RSGARDHERE
TEKRSSIPIT VRQLEAVVRI SESLGKMKLQ PFVTETDVEE ALRLFQVSTL DAAMSGSLSG
VEGFSTQEDQ EMLSRIEKQL KRRFAIGSQV SEHSIIQDFL KQKYPEHAIH KVLNLMMRRG
EIHHRLQRKV LYRLK
