MCM7B_XENLA
ID MCM7B_XENLA Reviewed; 720 AA.
AC Q7ZXB1; O42592;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=DNA replication licensing factor mcm7-B;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q61881};
DE AltName: Full=CDC47 homolog B;
DE AltName: Full=CDC47-2p;
DE AltName: Full=Minichromosome maintenance protein 7-B;
DE Short=xMCM7-B;
GN Name=mcm7-b; Synonyms=cdc47-2 {ECO:0000312|EMBL:AAC60228.1};
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:AAC60228.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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:AAH45072.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH45072.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-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. 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 (By similarity). {ECO:0000250|UniProtKB:P33993}.
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 Evidence={ECO:0000250|UniProtKB:Q61881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q61881};
CC -!- SUBUNIT: Component of the mcm2-7 complex (RLF-M) (By similarity). The
CC complex forms a toroidal hexameric ring with the proposed subunit order
CC mcm2-mcm6-mcm4-mcm7-mcm3-mcm5 (By similarity). The heterodimer of
CC mmcm3/mcm5 interacts with mcm4, mmcm6, mcm7 and weakly with mcm2 (By
CC similarity). The N-terminus is required for interaction with mmcm3,
CC though this interaction may not be direct, and remains in a complex
CC with mmcm3 throughout the cell cycle (By similarity). Begins to
CC associate with zmcm6 at the neurula stage (By similarity). Component of
CC the replisome complex (By similarity). Component of the CMG helicase
CC complex, composed of the mcm2-7 complex, the GINS complex and cdc45 (By
CC similarity). {ECO:0000250|UniProtKB:P33993}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91876}.
CC Chromosome {ECO:0000250|UniProtKB:Q91876}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:Q91876}.
CC -!- PTM: Ubiquitinated by traip when forks converge following formation of
CC DNA interstrand cross-links (By similarity). Short ubiquitin chains on
CC mcm7 promote recruitment of DNA glycosylase neil3 (By similarity). If
CC the interstrand cross-link cannot be cleaved by neil3, the ubiquitin
CC chains continue to grow on mcm7, promoting the unloading of the CMG
CC helicase complex by the vcp/p97 ATPase (By similarity).
CC {ECO:0000250|UniProtKB:P33993}.
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. Specifically a MCM467 subcomplex is shown to
CC have in vitro helicase activity which is inhibited by the MCM2 subunit.
CC The MCM2-7 hexamer is the proposed physiological active complex.
CC {ECO:0000250|UniProtKB:Q61881}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR EMBL; U66710; AAC60228.1; -; mRNA.
DR EMBL; BC045072; AAH45072.1; -; mRNA.
DR RefSeq; NP_001080722.1; NM_001087253.1.
DR AlphaFoldDB; Q7ZXB1; -.
DR SMR; Q7ZXB1; -.
DR BioGRID; 98656; 4.
DR IntAct; Q7ZXB1; 1.
DR MaxQB; Q7ZXB1; -.
DR PRIDE; Q7ZXB1; -.
DR DNASU; 380414; -.
DR GeneID; 380414; -.
DR KEGG; xla:380414; -.
DR CTD; 380414; -.
DR Xenbase; XB-GENE-6256533; mcm7.L.
DR OMA; NAYTCDR; -.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 380414; Expressed in egg cell and 19 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0071162; C:CMG complex; ISS: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:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:UniProtKB.
DR CDD; cd17758; MCM7; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008050; MCM7.
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 PANTHER; PTHR11630:SF26; PTHR11630:SF26; 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; PR01663; MCMPROTEIN7.
DR SMART; SM00382; AAA; 1.
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; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..720
FT /note="DNA replication licensing factor mcm7-B"
FT /id="PRO_0000240596"
FT DOMAIN 331..537
FT /note="MCM"
FT /evidence="ECO:0000255"
FT ZN_FING 183..210
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT MOTIF 512..515
FT /note="Arginine finger"
FT BINDING 380..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 46
FT /note="A -> T (in Ref. 1; AAC60228)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="E -> Q (in Ref. 1; AAC60228)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="E -> D (in Ref. 1; AAC60228)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="E -> Q (in Ref. 1; AAC60228)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="E -> D (in Ref. 1; AAC60228)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="E -> D (in Ref. 1; AAC60228)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="E -> Q (in Ref. 1; AAC60228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 81733 MW; 4DD83F5D573EE94D CRC64;
MPRDYQAEKE KCKTFLQEFY KDDEFGKKNF KYGVQLANIA HREQVALCID LDDLAEEDPE
LVDAICENTR RYTNLFADAV QELLPQYKER EVVHKDALDV YIEHRLMMEQ RGRDPNEMRD
PHNQYPPELM RRFELYFKAP SSSKARVVRD VKADSIGKLV TVRGIVTRVT EVKPMMVVAT
YTCDQCGAET YQPIQSPTFM PLIMCPSREC QTNRSGGRLY LQTRGSKFIK FQELKIQEHS
DQVPVGNIPR CMSVYVRGEN TRLAQPGDHV GITGVFLPML RTGFRQVVQG LLSETYLESH
RLVKMNKTED DELGTEELSE EELRQITEED FYEKLAASIA PEIYGHEDVK KALLLLLVGG
VDHSPRGMKI RGNINVCLMG DPGVAKSQLL SYIDRLAPRS QYTTGRGSSG VGLTAAVMKD
PVTGEMTLEG GALVLADQGV CCIDEFDKMM DSDRTAIHEV MEQQTISIAK AGIMTTLNAR
CSILAAANPA YGRYNPKKTV EQNIQLPAAL LSRFDLLWLI QDKPDRDNDL RLAQHITYVH
QHSKQPPSQF QPMDMKLMRR YITMCKSKQP AIPESLADYL TAAYVEMRKE ARTNKDMTFT
SARTLLSILR LSTALARLRL EDVVEKEDVN EAMRLTEMSK DSLQGDKGHA SRTQRPADVI
FSTIREMVPE KGARSVKYSE AEQRCVSKGF TPAQFEAALE EYEELNVWLV NQARTKITFV
