MCM5A_XENLA
ID MCM5A_XENLA Reviewed; 735 AA.
AC P55862; Q5D0A3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=DNA replication licensing factor mcm5-A {ECO:0000305};
DE Short=xMCM5-A;
DE EC=3.6.4.12;
DE AltName: Full=CDC46 homolog A;
DE Short=xCDC46-A {ECO:0000305|PubMed:8917078};
DE AltName: Full=CDC46p;
DE AltName: Full=p92;
GN Name=mcm5-a; Synonyms=cdc46-a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH
RP MCM2; MMCM3; MCM4; MMCM6 AND MCM7, AND SUBCELLULAR LOCATION.
RC TISSUE=Oocyte;
RX PubMed=9214647; DOI=10.1093/emboj/16.11.3320;
RA Kubota Y., Mimura S., Nishimoto S., Masuda T., Nojima H., Takisawa H.;
RT "Licensing of DNA replication by a multi-protein complex of MCM/P1 proteins
RT in Xenopus eggs.";
RL EMBO J. 16:3320-3331(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-735, AND IDENTIFICATION IN A COMPLEX WITH
RP MCM2.
RC TISSUE=Oocyte;
RX PubMed=8917078; DOI=10.1016/0378-1119(96)00122-9;
RA Miyake S., Saito I., Kobayashi H., Yamashita S.;
RT "Identification of two Xenopus laevis genes, xMCM2 and xCDC46, with
RT sequence homology to MCM genes involved in DNA replication.";
RL Gene 175:71-75(1996).
RN [4]
RP FUNCTION, IDENTIFICATION IN RLF-M COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=9214646; DOI=10.1093/emboj/16.11.3312;
RA Thommes P., Kubota Y., Takisawa H., Blow J.J.;
RT "The RLF-M component of the replication licensing system forms complexes
RT containing all six MCM/P1 polypeptides.";
RL EMBO J. 16:3312-3319(1997).
RN [5]
RP IDENTIFICATION IN MCM COMPLEXES.
RX PubMed=9851868; DOI=10.1006/excr.1998.4271;
RA Coue M., Amariglio F., Maiorano D., Bocquet S., Mechali M.;
RT "Evidence for different MCM subcomplexes with differential binding to
RT chromatin in Xenopus.";
RL Exp. Cell Res. 245:282-289(1998).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH MCM2; MMCM3; MCM4; MMCM6 AND
RP MCM7.
RX PubMed=16369567; DOI=10.1038/sj.emboj.7600892;
RA Ying C.Y., Gautier J.;
RT "The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is
RT required for DNA unwinding.";
RL EMBO J. 24:4334-4344(2005).
RN [7]
RP IDENTIFICATION IN THE CMG HELICASE COMPLEX.
RX PubMed=30979826; DOI=10.26508/lsa.201900390;
RA Priego Moreno S., Jones R.M., Poovathumkadavil D., Scaramuzza S.,
RA Gambus A.;
RT "Mitotic replisome disassembly depends on TRAIP ubiquitin ligase
RT activity.";
RL Life. Sci Alliance 2:0-0(2019).
RN [8]
RP IDENTIFICATION IN THE CMG HELICASE COMPLEX.
RX PubMed=30842657; DOI=10.1038/s41586-019-1002-0;
RA Wu R.A., Semlow D.R., Kamimae-Lanning A.N., Kochenova O.V., Chistol G.,
RA Hodskinson M.R., Amunugama R., Sparks J.L., Wang M., Deng L., Mimoso C.A.,
RA Low E., Patel K.J., Walter J.C.;
RT "TRAIP is a master regulator of DNA interstrand crosslink repair.";
RL Nature 567:267-272(2019).
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:0000269|PubMed:16369567, ECO:0000269|PubMed:9214646,
CC ECO:0000269|PubMed:9214647}.
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) (PubMed:16369567,
CC PubMed:8917078, PubMed:9214646, PubMed:9214647, PubMed:9851868). The
CC complex forms a toroidal hexameric ring with the proposed subunit order
CC mcm2-mcm6-mcm4-mcm7-mcm3-mcm5 (PubMed:16369567, PubMed:8917078,
CC PubMed:9214646, PubMed:9214647, PubMed:9851868). The heterodimer of
CC mmcm3/mcm5 interacts with mcm4, mmcm6, mcm7 and weakly with mcm2
CC (PubMed:16369567, PubMed:8917078, PubMed:9214646, PubMed:9214647,
CC PubMed:9851868). Component of the CMG helicase complex, composed of the
CC mcm2-7 complex, the GINS complex and cdc45 (PubMed:30979826,
CC PubMed:30842657). {ECO:0000269|PubMed:16369567,
CC ECO:0000269|PubMed:30842657, ECO:0000269|PubMed:30979826,
CC ECO:0000269|PubMed:8917078, ECO:0000269|PubMed:9214646,
CC ECO:0000269|PubMed:9214647, ECO:0000269|PubMed:9851868}.
CC -!- INTERACTION:
CC P55862; P49739: mmcm3; NbExp=5; IntAct=EBI-876879, EBI-491720;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9214646,
CC ECO:0000269|PubMed:9214647}. Chromosome {ECO:0000269|PubMed:9214646,
CC ECO:0000269|PubMed:9214647}. Note=Associated with chromatin before the
CC formation of nuclei and detaches from it as DNA replication progresses.
CC {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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; U44048; AAC60224.1; -; mRNA.
DR EMBL; D63920; BAA09949.1; -; mRNA.
DR EMBL; BC047250; AAH47250.1; -; mRNA.
DR PIR; T47224; PC4225.
DR RefSeq; NP_001080893.1; NM_001087424.1.
DR AlphaFoldDB; P55862; -.
DR SMR; P55862; -.
DR BioGRID; 98829; 2.
DR ComplexPortal; CPX-2943; MCM complex.
DR IntAct; P55862; 6.
DR MINT; P55862; -.
DR MaxQB; P55862; -.
DR DNASU; 380587; -.
DR GeneID; 380587; -.
DR KEGG; xla:380587; -.
DR CTD; 380587; -.
DR Xenbase; XB-GENE-6256510; mcm5.L.
DR OMA; ITYCKTR; -.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 380587; Expressed in neurula embryo and 18 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0071162; C:CMG complex; IDA:UniProtKB.
DR GO; GO:0042555; C:MCM complex; IDA: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; IDA:UniProtKB.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA: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 1: Evidence at protein 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-A"
FT /id="PRO_0000194109"
FT DOMAIN 332..538
FT /note="MCM"
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; 82435 MW; 702BA90C2F510720 CRC64;
MSGFDDLGVY YSDSFGGEQQ VGDDGQAKKS QLKKRFREFL RQYRIGTDRT GFTFKYRDEL
KRHYNLGEYW IEVEMEDLAS FDEDLADYLY KQPTEHLQLL EEAAQEVADE VTRPRPAGEE
TIQEIQVMLR SDANPANIRS LKSEQMSHLV KIPGIIIAAT AVRAKATKIS IQCRSCRNTI
GNIAVRPGLE GYAMPRKCNT EQAGRPNCPL DPYFIIPDKC KCVDFQTLKL QESPDAVPHG
ELPRHMQLYC DRYLCDKVVP GNRVTIMGIY SIRKSGKTST KGRDRVGVGI RSSYIRVVGI
QVDTEGTGRS AAGAITPQEE EEFRRLAAKP DIYETVAKSI APSIYGSSDI KKAIACLLFG
GSRKRLPDGL TRRGDVNLLM LGDPGTAKSQ LLKFVERCSP IGVYTSGKGS SAAGLTASVM
RDPVSRNFIM EGGAMVLADG GVVCIDEFDK MREDDRVAIH EAMEQQTISI AKAGITTTLN
SRCSVLAAAN SVYGRWDDTK GEENIDFMPT ILSRFDMIFI VKDEHNEQRD MTLAKHVMNV
HLSARTQSSS VEGEVDLNTL KKYIAYCRAK CGPRLSAEAA EKLKNRYILM RSGAREHERE
TEKRSSIPIT VRQLEAIVRI SESLGKMKLQ PFATETDVEE ALRLFQVSTL DAAMSGSLSG
VEGFTTQEDQ EMLSRIEKQM KKRFAIGSQV SEHSIIQDFL KQKYPEHAIH KVLSLMMRRG
EIQHRLQRKV LYRIK
