MCM5_XENTR
ID MCM5_XENTR Reviewed; 735 AA.
AC Q561P5; Q28DV1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DNA replication licensing factor mcm5 {ECO:0000250|UniProtKB:P33992};
DE EC=3.6.4.12;
GN Name=mcm5 {ECO:0000312|EMBL:AAH93455.1}; ORFNames=TEgg011k14.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ81496.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAJ81496.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2005) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q561P5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q561P5-2; Sequence=VSP_052071, VSP_052072;
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR EMBL; CR848584; CAJ81496.1; -; mRNA.
DR EMBL; BC093455; AAH93455.1; -; mRNA.
DR RefSeq; NP_001017327.2; NM_001017327.3. [Q561P5-1]
DR AlphaFoldDB; Q561P5; -.
DR SMR; Q561P5; -.
DR PaxDb; Q561P5; -.
DR GeneID; 550081; -.
DR KEGG; xtr:550081; -.
DR CTD; 4174; -.
DR Xenbase; XB-GENE-985665; mcm5.
DR eggNOG; KOG0481; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q561P5; -.
DR OMA; FLEIDIM; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q561P5; -.
DR TreeFam; TF105653; -.
DR Reactome; R-XTR-176187; Activation of ATR in response to replication stress.
DR Reactome; R-XTR-68867; Assembly of the pre-replicative complex.
DR Reactome; R-XTR-68962; Activation of the pre-replicative complex.
DR Reactome; R-XTR-69052; Switching of origins to a post-replicative state.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000000253; Expressed in egg cell and 11 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: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:0006268; P:DNA unwinding involved in DNA replication; ISS:UniProtKB.
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; 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 Alternative splicing; ATP-binding; Cell cycle; Chromosome; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..735
FT /note="DNA replication licensing factor mcm5"
FT /id="PRO_0000239941"
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"
FT VAR_SEQ 452..471
FT /note="REDDRVAIHEAMEQQTISIA -> QGVVIVHLPSSLTAKWEGSK (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_052071"
FT VAR_SEQ 472..735
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_052072"
SQ SEQUENCE 735 AA; 82510 MW; E050823A9D99A14F CRC64;
MSGFDDLGIY YSDSFGGEQP VGDDGQAKKS QLKKRFREFL RQYRVGTDRT GFTFKYRDEL
KRHYNLGEYW IEVEMEDLAS FDEDLADYLY KQPTEHLQLL EEAAQEVADE VTRPRPAGEE
TIQEIQVMLR SDANPANIRS LKSEQMSHLV KIPGIIIAAT AVRAKATKIS IQCRSCRNTI
GNIAVRPGLE GYAMPRKCNT EQAGRPKCPL DPYFIIPDKC KCVDFQTLKL QESPDAVPHG
ELPRHMQLYC DRYLCDKVVP GNRVTIMGIY SIRKSGKTST KGRDRVGVGI RSSYIRVVGI
QVDTEGTGRS AAGAITPQEE EEFRRLSAKP DIYETVAKSI APSIYGSSDI KKAIACLLFG
GSRKRLPDGL TRRGDVNLLM LGDPGTAKSQ LLKFVERCSP IGVYTSGKGS SAAGLTASVM
RDPVSRNFIM EGGAMVLADG GVVCIDEFDK MREDDRVAIH EAMEQQTISI AKAGITTTLN
SRCSVLAAAN SVYGRWDDTK GEENIDFMPT ILSRFDMIFI VKDEHNEQRD MTLAKHVMNV
HLSARTQSSS VEGEIDLNTL KKYIAYCRAK CGPRLSAESA EKLKNRYILM RSGARDHERE
TEKRSSIPIT VRQLEAIVRI SESLGKMKLQ PFATETDVEE ALRLFQVSTL DAAMSGSLSG
VEGFTTQEDQ EMLSRIEKQL KRRFAIGSQV SEHSIIQDFL KQKYPEHAIH KVLHLMMRRG
EIQHRLQRKV LYRIK
