MCM7_SCHPO
ID MCM7_SCHPO Reviewed; 760 AA.
AC O75001; P87302;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=DNA replication licensing factor mcm7;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance protein 7;
GN Name=mcm7; ORFNames=SPBC25D12.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=SP011;
RX PubMed=11606526; DOI=10.1093/genetics/159.2.471;
RA Liang D.T., Forsburg S.L.;
RT "Characterization of Schizosaccharomyces pombe mcm7(+) and cdc23(+) (MCM10)
RT and interactions with replication checkpoints.";
RL Genetics 159:471-486(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 367-466.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9366552; DOI=10.1046/j.1365-2443.1997.1350333.x;
RA Adachi Y., Usukura J., Yanagida M.;
RT "A globular complex formation by Nda1 and the other five members of the MCM
RT protein family in fission yeast.";
RL Genes Cells 2:467-479(1997).
RN [4]
RP INTERACTION WITH SLD3.
RX PubMed=12006645; DOI=10.1091/mbc.02-01-0006;
RA Nakajima R., Masukata H.;
RT "SpSld3 is required for loading and maintenance of SpCdc45 on chromatin in
RT DNA replication in fission yeast.";
RL Mol. Biol. Cell 13:1462-1472(2002).
RN [5]
RP INTERACTION WITH MCM10.
RX PubMed=12604790; DOI=10.1073/pnas.0237384100;
RA Lee J.-K., Seo Y.-S., Hurwitz J.;
RT "The Cdc23 (Mcm10) protein is required for the phosphorylation of
RT minichromosome maintenance complex by the Dfp1-Hsk1 kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2334-2339(2003).
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 (By similarity).
CC Required for the progression of S phase. {ECO:0000250,
CC ECO:0000269|PubMed:11606526}.
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. The complex forms a toroidal
CC hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-mcm7-
CC mcm3-mcm5 (Probable). The heterodimers of mcm4/mcm6 and mcm3/mcm5
CC interact with mcm2 and mcm7. Interacts with sld3 and mcm10.
CC {ECO:0000269|PubMed:11606526, ECO:0000269|PubMed:12006645,
CC ECO:0000269|PubMed:12604790, ECO:0000305}.
CC -!- INTERACTION:
CC O75001; O94450: SPAC1687.04; NbExp=2; IntAct=EBI-913851, EBI-7492115;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11606526}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AF070481; AAC23693.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20099.1; -; Genomic_DNA.
DR EMBL; AJ000065; CAA03898.1; -; Genomic_DNA.
DR PIR; T39991; T39991.
DR RefSeq; NP_596545.1; NM_001022466.2.
DR AlphaFoldDB; O75001; -.
DR SMR; O75001; -.
DR BioGRID; 277156; 19.
DR ComplexPortal; CPX-2945; MCM complex.
DR IntAct; O75001; 5.
DR MINT; O75001; -.
DR STRING; 4896.SPBC25D12.03c.1; -.
DR iPTMnet; O75001; -.
DR MaxQB; O75001; -.
DR PaxDb; O75001; -.
DR PRIDE; O75001; -.
DR EnsemblFungi; SPBC25D12.03c.1; SPBC25D12.03c.1:pep; SPBC25D12.03c.
DR GeneID; 2540630; -.
DR KEGG; spo:SPBC25D12.03c; -.
DR PomBase; SPBC25D12.03c; mcm7.
DR VEuPathDB; FungiDB:SPBC25D12.03c; -.
DR eggNOG; KOG0482; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; O75001; -.
DR OMA; NAYTCDR; -.
DR PhylomeDB; O75001; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR Reactome; R-SPO-69052; Switching of origins to a post-replicative state.
DR PRO; PR:O75001; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IC:PomBase.
DR GO; GO:0042555; C:MCM complex; IDA:PomBase.
DR GO; GO:0097373; C:MCM core complex; IDA:PomBase.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IC:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
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: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; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; EXP:PomBase.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..760
FT /note="DNA replication licensing factor mcm7"
FT /id="PRO_0000194123"
FT DOMAIN 353..559
FT /note="MCM"
FT MOTIF 535..538
FT /note="Arginine finger"
FT BINDING 403..410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 457
FT /note="V -> I (in Ref. 3; CAA03898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 85622 MW; 2141F8F9CB0BAA34 CRC64;
MALPTIDLKI PEYEECQHKI TDFLSHFKQE QVQDGQQNQD ISMSDAGDEP FLKSKYMDIL
QKISNRESNV INVDLNDLYE FDPSDTQLLH NIESNAKRFV ELFSQCADAL MPPPTVEINY
RNEVLDVIMQ QRVQRNENID PEHKGFPPEL TRGYDLYFRP VTRNKKPFSV RDLRGENLGS
LLTVRGIVTR TSDVKPSLTV NAYTCDRCGY EVFQEIRQKT FLPMSECPSD ECKKNDAKGQ
LFMSTRASKF LPFQEVKIQE LTNQVPIGHI PRSLTVHLYG AITRSVNPGD IVDISGIFLP
TPYTGFRAMR AGLLTDTYLE CHYVSQIIKN YTNIEKTPQS EAAIAELNQG GNVYEKLAKS
IAPEIYGHED VKKALLLLLV GGVTKELGDG MRIRGDINIC LTGDPGVAKS QLLKYISKVA
PRGVYTTGRG SSGVGLTAAV MRDPVTDEMV LEGGALVLAD NGICCIDEFD KMDESDRTAI
HEVMEQQTIS ISKAGITTTL NARTSILAAA NPLYGRYNPK VAPIHNINLP AALLSRFDIL
FLILDTPSRE TDEHLAQHVT YVHMHNEQPK MDFEPLDPNM IRHYISSARQ YRPVVPKDVC
DYVTGAYVQL RQNQKRDEAN ERQFAHTTPR TLLAILRMGQ ALARLRFSNR VEIGDVDEAL
RLMSVSKSSL YDDLDPSSHD TTITSKIYKI IRDMLNSIPD VEGNERSLTL RAIRERVLAK
GFTEDHLINT IQEYTDLGVL LTTNNGQTIM FLDPDLHMEN
