MCM7_XENTR
ID MCM7_XENTR Reviewed; 720 AA.
AC Q6NX31;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DNA replication licensing factor mcm7;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q61881};
DE AltName: Full=CDC47 homolog;
DE AltName: Full=Minichromosome maintenance protein 7;
GN Name=mcm7 {ECO:0000312|EMBL:AAH67307.1}; ORFNames=TGas137h09.1;
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:AAH67307.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAH67307.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH67307.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2004) 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:Q91876}.
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). 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. The N-terminus is required for
CC interaction with mmcm3, though this interaction may not be direct, and
CC remains in a complex with mmcm3 throughout the cell cycle. 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 ECO:0000250|UniProtKB:Q91876}.
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. Short ubiquitin chains on mcm7 promote
CC recruitment of DNA glycosylase neil3. If the interstrand cross-link
CC cannot be cleaved by neil3, the ubiquitin chains continue to grow on
CC mcm7, promoting the unloading of the CMG helicase complex by the
CC vcp/p97 ATPase. {ECO:0000250|UniProtKB:Q91876}.
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; CR855766; CAJ83441.1; -; mRNA.
DR EMBL; BC067307; AAH67307.1; -; mRNA.
DR RefSeq; NP_998877.1; NM_213712.1.
DR AlphaFoldDB; Q6NX31; -.
DR SMR; Q6NX31; -.
DR PRIDE; Q6NX31; -.
DR DNASU; 407945; -.
DR Ensembl; ENSXETT00000074596; ENSXETP00000065628; ENSXETG00000009104.
DR GeneID; 407945; -.
DR KEGG; xtr:407945; -.
DR CTD; 4176; -.
DR Xenbase; XB-GENE-5946446; mcm7.
DR InParanoid; Q6NX31; -.
DR OrthoDB; 266497at2759; -.
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 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000009104; Expressed in 4-cell stage embryo and 14 other tissues.
DR ExpressionAtlas; Q6NX31; baseline.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006271; P:DNA strand elongation involved in DNA replication; 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 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"
FT /id="PRO_0000240597"
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"
SQ SEQUENCE 720 AA; 81762 MW; 95E2495E4C771D09 CRC64;
MPRDYQAEKE KCKTFLQEFY KDDELGKKNF KYGVQLANIA HREQVALYID LDDLAEEDPE
LVDAICENTR RYTNLFADAV QELLPQYKER EVVHKDALDV YIEHRLMMEQ RGRDPSETRD
PHNQYPPELM RRFELYFKAP SSSKARVVRD VKADSIGKLV TVRGIVTRVT EVKPMMVVAT
YTCDQCGAET YQPIQSPTFM PLIMCPSREC QTNRSGGRLY LQTRGSKFIK FQELKIQEHS
DQVPVGNIPR CMSVYVRGEN TRLAQPGDHV SITGVFLPML RTGFRQVVQG LLSETYLESH
RLVKMNKTED DELGTEELSE EELRQITEED FYEKLAASIA PEIYGHEDVK KALLLLLVGG
VDNSPRGMKI RGNINICLMG DPGVAKSQLL SYIDRLAPRS QYTTGRGSSG VGLTAAVMKD
PVTGEMTLEG GALVLADQGV CCIDEFDKMM DTDRTAIHEV MEQQTISIAK AGIMTTLNAR
CSILAAANPA YGRYNPKKTV EQNIQLPAAL LSRFDLLWLI QDKPDRDNDL RLAQHITYVH
QHSKQPPSQF QPLDMKLMRR YITMCKRKQP AIPESLADYL TAAYVEMRKE ARTNKDMTFT
SARTLLSILR LSTALARLRL EDVVEKEDVN EAMRLTEMSK DSLLGDKGQT SRTQRPADVI
FSTIREMVPE KGARSVKYSE AEQRAVSKGF TPAQFEAALE EYEELNVWLV NQARTKITFV
