MCM2_SCHPO
ID MCM2_SCHPO Reviewed; 830 AA.
AC P40377;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=DNA replication licensing factor mcm2;
DE EC=3.6.4.12;
DE AltName: Full=Cell division control protein 19;
DE AltName: Full=Minichromosome maintenance protein 2;
GN Name=mcm2; Synonyms=cdc19, nda1; ORFNames=SPBC4.04c;
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].
RX PubMed=7876346; DOI=10.1242/jcs.107.10.2779;
RA Forsburg S.L., Nurse P.;
RT "The fission yeast cdc19+ gene encodes a member of the MCM family of
RT replication proteins.";
RL J. Cell Sci. 107:2779-2788(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8298187; DOI=10.1091/mbc.4.10.1003;
RA Miyake S., Okishio N., Samejima I., Hiraoka Y., Toda T., Saitoh I.,
RA Yanagida M.;
RT "Fission yeast genes nda1+ and nda4+, mutations of which lead to S-phase
RT block, chromatin alteration and Ca2+ suppression, are members of the
RT CDC46/MCM2 family.";
RL Mol. Biol. Cell 4:1003-1015(1993).
RN [3]
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 [4]
RP SUBUNIT.
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 [5]
RP 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). Plays
CC an important role in DNA replication. {ECO:0000250}.
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 mcm10.
CC {ECO:0000269|PubMed:11606526, ECO:0000305}.
CC -!- INTERACTION:
CC P40377; P50582: hsk1; NbExp=2; IntAct=EBI-783248, EBI-908476;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; U08048; AAC48930.1; -; Genomic_DNA.
DR EMBL; S68468; AAC60569.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB58403.1; -; Genomic_DNA.
DR PIR; B48723; B48723.
DR RefSeq; NP_595477.1; NM_001021388.2.
DR AlphaFoldDB; P40377; -.
DR SMR; P40377; -.
DR BioGRID; 277146; 38.
DR ComplexPortal; CPX-2945; MCM complex.
DR IntAct; P40377; 8.
DR MINT; P40377; -.
DR STRING; 4896.SPBC4.04c.1; -.
DR iPTMnet; P40377; -.
DR MaxQB; P40377; -.
DR PaxDb; P40377; -.
DR PRIDE; P40377; -.
DR EnsemblFungi; SPBC4.04c.1; SPBC4.04c.1:pep; SPBC4.04c.
DR GeneID; 2540620; -.
DR KEGG; spo:SPBC4.04c; -.
DR PomBase; SPBC4.04c; mcm2.
DR VEuPathDB; FungiDB:SPBC4.04c; -.
DR eggNOG; KOG0477; Eukaryota.
DR HOGENOM; CLU_000995_0_0_1; -.
DR InParanoid; P40377; -.
DR OMA; DCVKCGY; -.
DR PhylomeDB; P40377; -.
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:P40377; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; 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: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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003688; F:DNA replication origin binding; ISO:PomBase.
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: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; IBA:GO_Central.
DR GO; GO:1905775; P:negative regulation of DNA helicase activity; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IC:PomBase.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008045; MCM2.
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:SF44; PTHR11630:SF44; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF12619; MCM2_N; 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; PR01658; MCMPROTEIN2.
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 Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..830
FT /note="DNA replication licensing factor mcm2"
FT /id="PRO_0000194092"
FT DOMAIN 484..691
FT /note="MCM"
FT ZN_FING 334..360
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 666..669
FT /note="Arginine finger"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 534..541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 830 AA; 92831 MW; A5BF0AA29661BD66 CRC64;
MDSFRKRGRR DSESLPFESE NSSLGATPLS LPPSSPPPEF SDEAAEALVE EDIEDLDGEA
LDVEDEEGED LFGEGMERDY QQNLELDRYD IEELDDDNDL EELDIGARRA VDARLRRRDI
ELDAAAGRTK PAAFLQDEDD DLDSNLGTGF TRHRHRIYDE YSPNVGALDE SGELPLESIA
DVKADSIAEW VTLDPVRRTI AREFKNFLLE YTDENGTSVY GNRIRTLGEV NAESLMVNYA
HLGESKPILA YFLANAPAPI FRIFDRVALE ATLLHYPDYE RIHSDIHVRI TNLPTCFTLR
DLRQSHLNCL VRVSGVVTRR TGLFPQLKYI RFTCTKCGAT LGPFFQDSSV EVKISFCHNC
SSRGPFVINS ERTVYNNYQR ITLQESPGTV PSGRLPRHRE VILLADLVDV AKPGEEIDVT
GIYRNNFDAS LNTKNGFPVF ATIIEANHIS QLDGSGNTDD DFSLSRLTDD EEREIRALAK
SPDIHNRIIA SMAPSIYGHR SIKTAIAAAL FGGVPKNING KHKIRGDINV LLLGDPGTAK
SQFLKYVEKT AHRAVFATGQ GASAVGLTAS VRKDPITNEW TLEGGALVLA DKGVCLIDEF
DKMNDQDRTS IHEAMEQQSI SISKAGIVTT LQARCTIIAA ANPIGGRYNT TIPFNQNVEL
TEPILSRFDI LQVVKDTVNP EIDEQLANFV VSSHIRSHPA FDPNMDVLKK VPTETGIDAK
PIPQDLLRKY IHFAREKVFP RLQQMDEEKI SRLYSDMRRE SLATGSYPIT VRHLESAIRL
SEAFAKMQLS EFVRPSHIDK AIQVIIDSFV NAQKMSVKRS LSRTFAKYLI
