MCM6M_XENLA
ID MCM6M_XENLA Reviewed; 821 AA.
AC Q5FWY4; O42590;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Maternal DNA replication licensing factor mcm6;
DE EC=3.6.4.12;
DE AltName: Full=Maternal minichromosome maintenance protein 6;
DE Short=mMCM6;
DE Short=xMCM6;
GN Name=mmcm6 {ECO:0000303|PubMed:9512418};
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:0000305, ECO:0000312|EMBL:AAC60226.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH
RP MCM2; MMCM3; MCM4; MCM5 AND MCM7, AND SUBCELLULAR LOCATION.
RC TISSUE=Oocyte {ECO:0000269|PubMed:9214647};
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] {ECO:0000312|EMBL:AAH89118.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg {ECO:0000312|EMBL:AAH89118.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=9512418; DOI=10.1016/s0960-9822(98)70136-8;
RA Sible J.C., Erikson E., Hendrickson M., Maller J.L., Gautier J.;
RT "Developmental regulation of MCM replication factors in Xenopus laevis.";
RL Curr. Biol. 8:347-350(1998).
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] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH MCM2; MMCM3; MCM4; MCM5 AND
RP MCM7, AND MUTAGENESIS OF LYS-404.
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. The existence of
CC maternal and zygotic forms of mcm3 and mcm6 suggests that specific
CC forms of mcm2-7 complexes may be used during different stages of
CC development. {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:9214646, PubMed:9214647, PubMed:9851868). The complex forms a
CC toroidal hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-
CC mcm7-mcm3-mcm5 (PubMed:16369567, PubMed:9214646, PubMed:9214647,
CC PubMed:9851868). The heterodimer of mmcm3/mcm5 interacts with mcm4,
CC mmcm6, mcm7 and weakly with mcm2 (PubMed:16369567, PubMed:9214646,
CC PubMed:9214647, PubMed:9851868). Component of the CMG helicase complex,
CC composed of the mcm2-7 complex, the GINS complex and cdc45
CC (PubMed:30979826, PubMed:30842657). {ECO:0000269|PubMed:16369567,
CC ECO:0000269|PubMed:30842657, ECO:0000269|PubMed:30979826,
CC ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647,
CC ECO:0000269|PubMed:9851868}.
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 -!- DEVELOPMENTAL STAGE: Expressed maternally. Expressed in the egg and
CC early embryo at a constant level until the gastrula stage, declining
CC drastically at the neurula stage. {ECO:0000269|PubMed:9512418}.
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; U44050; AAC60226.1; -; mRNA.
DR EMBL; BC089118; AAH89118.1; -; mRNA.
DR PIR; T47222; T47222.
DR RefSeq; NP_001081822.1; NM_001088353.1.
DR AlphaFoldDB; Q5FWY4; -.
DR SMR; Q5FWY4; -.
DR BioGRID; 99406; 2.
DR IntAct; Q5FWY4; 2.
DR MaxQB; Q5FWY4; -.
DR DNASU; 398071; -.
DR GeneID; 398071; -.
DR KEGG; xla:398071; -.
DR CTD; 398071; -.
DR Xenbase; XB-GENE-5870555; mcm6.2.L.
DR OMA; VQDENMA; -.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR008049; MCM6.
DR InterPro; IPR041024; Mcm6_C.
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; PF18263; MCM6_C; 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; PR01662; MCMPROTEIN6.
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; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..821
FT /note="Maternal DNA replication licensing factor mcm6"
FT /id="PRO_0000235887"
FT DOMAIN 348..555
FT /note="MCM"
FT /evidence="ECO:0000255"
FT ZN_FING 160..187
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 665..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 530..533
FT /note="Arginine finger"
FT COMPBIAS 680..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398..405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 404
FT /note="K->A: Reduces ATPase activity of the mcm2-mcm7
FT complex by 50% and disrupts DNA replication. Does not
FT disrupt formation of the pre-replicative complex onto
FT chromatin. Abolishes ATPase activity of the mcm2-mcm7
FT complex; when associated with A-386 in mcm7."
FT /evidence="ECO:0000269|PubMed:16369567"
FT CONFLICT 36
FT /note="L -> F (in Ref. 1; AAC60226)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="L -> F (in Ref. 1; AAC60226)"
FT /evidence="ECO:0000305"
FT CONFLICT 786..821
FT /note="ELNKSELKTMDDTKETGEDAAEDRILVVNPNYMLED -> RTEQIGIKNNG
FT (in Ref. 1; AAC60226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 92639 MW; 68916B7363974731 CRC64;
MELGGPAAAG DTDIAGQQLF KDELSDKCQK LFLEFLEECK GKDGSNLYVS AAEELIRPER
NTLAVNFTDI EYYNQQLATT IQEEYYRVYP HLCRAVRSFA RQMGNIPANK EFYIAFSDFP
ARQKIRELSS AKIGTLLRIS GQVVRTHPVH PELVSGTFLC MDCQSIVKDV EQQFRYTQPT
ICKNPVCANR RRFTLDTNKS RFVDFQKVRI QETQAELPRG AIPRSVEIIL RAEAVESAMA
GDRCDFTGTL IVVPDVSALA AGDARMETGA KVTGGEGFNS EGVQGLKALG VRDLSYRLAF
LACYVGATNP RFGGKDLREE DQTAESIKNQ MTVQEWEKVF EMSQDKNLYH NLCTSLFPTI
HGNDEIKRGV LLMLFGGVPK TTMEGTSLRG DINVCIVGDP STSKSQFLKH VEEFSPRAVY
TSGKASSAAG LTAAVVKDEE SHEFVIEAGA LMLADNGVCC IDEFDKMDLK DQVAIHEAME
QQTISITKAG VKATLNARTS ILAAANPVGG RYERSKSLKH NVNLSAPIMS RFDLFFILVD
ECNEVTDYAI ARRIVDLHAR NEESIERVYS IEDIQRYLLF ARQFQPKITK EAEEFIVEQY
RRLRQRDGSG VAKSSWRITV RQLESLIRLS ESMARMHCSD EVQPKHVKEA FRLLSKSIIR
VDTPDVSFDQ GEDEKNIEGE NNGNLNNGEE AMETNQDEPI NEKPSSNAGL KMSFAEYKQI
SNLLVLYMQK MEETEEECHL TTTDLVNWYL KEMEAEIETE TELILKKRLI EKVIHRLIYY
DHILIELNKS ELKTMDDTKE TGEDAAEDRI LVVNPNYMLE D
