MCM10_SCHPO
ID MCM10_SCHPO Reviewed; 593 AA.
AC O42709;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=DNA replication licensing factor mcm10;
DE AltName: Full=Cdc23 protein;
DE AltName: Full=Minichromosome maintenance protein 10;
GN Name=mcm10; Synonyms=cdc23; ORFNames=SPBC1347.10;
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], AND FUNCTION.
RX PubMed=9745018; DOI=10.1007/s002940050382;
RA Aves S.J., Tongue N., Foster A.J., Hart E.A.;
RT "The essential Schizosaccharomyces pombe cdc23 DNA replication gene shares
RT structural and functional homology with the Saccharomyces cerevisiae DNA43
RT (MCM10) gene.";
RL Curr. Genet. 34:164-171(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10783164;
RA Homesley L., Lei M., Kawasaki Y., Sawyer S., Christensen T., Tye B.K.;
RT "Mcm10 and the MCM2-7 complex interact to initiate DNA synthesis and to
RT release replication factors from origins.";
RL Genes Dev. 14:913-926(2000).
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 FUNCTION, INTERACTION WITH HIM1; HSK1; MCM2 AND MCM7, AND INTERACTION WITH
RP THE MCM2-7 COMPLEX AND THE DFP1-HSK1 COMPLEX.
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).
RN [5]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH POL1.
RX PubMed=14766746; DOI=10.1074/jbc.m400142200;
RA Fien K., Cho Y.-S., Lee J.-K., Raychaudhuri S., Tappin I., Hurwitz J.;
RT "Primer utilization by DNA polymerase alpha-primase is influenced by its
RT interaction with Mcm10p.";
RL J. Biol. Chem. 279:16144-16153(2004).
RN [6]
RP INTERACTION WITH ABP1.
RX PubMed=17112379; DOI=10.1186/1747-1028-1-27;
RA Locovei A.M., Spiga M.-G., Tanaka K., Murakami Y., D'Urso G.;
RT "The CENP-B homolog, Abp1, interacts with the initiation protein Cdc23
RT (MCM10) and is required for efficient DNA replication in fission yeast.";
RL Cell Div. 1:27-27(2006).
RN [7]
RP FUNCTION AS A PRIMASE, AND MUTAGENESIS OF GLU-586; ASP-587 AND ASP-588.
RX PubMed=16720577; DOI=10.1074/jbc.m512997200;
RA Fien K., Hurwitz J.;
RT "Fission yeast Mcm10p contains primase activity.";
RL J. Biol. Chem. 281:22248-22260(2006).
CC -!- FUNCTION: Required for DNA synthesis. Required for entry into or
CC completion of S phase. Involved in DNA replication and seems to
CC participate in the activation of the pre-replication complex (pre-RC)
CC and in transcription elongation. May play a role as key coordinator in
CC assembling the replication fork. Proposed to function at replication
CC origins following the binding of the mcm2-7 complex prior to the
CC recruitment of sna41. Probably is required to stimulate phosphorylation
CC of the mcm2-7 complex by the dfp1-hsk1 kinase complex. May recruit the
CC DNA polymerase alpha:primase complex to replication origins and is
CC required to maintain it on chromatin independently of sna41. May have
CC primase activity. Binds to single-stranded DNA.
CC {ECO:0000269|PubMed:10783164, ECO:0000269|PubMed:12604790,
CC ECO:0000269|PubMed:14766746, ECO:0000269|PubMed:16720577,
CC ECO:0000269|PubMed:9745018}.
CC -!- SUBUNIT: Self-associates (By similarity). Interacts with mcm2, mcm7,
CC him1/dfp1, hsk1, pol1 and abp1. Associates with the mcm2-7 complex and
CC the dfp1-hsk1 complex. {ECO:0000250, ECO:0000269|PubMed:10783164,
CC ECO:0000269|PubMed:12604790, ECO:0000269|PubMed:14766746,
CC ECO:0000269|PubMed:17112379}.
CC -!- INTERACTION:
CC O42709; P50582: hsk1; NbExp=3; IntAct=EBI-1387246, EBI-908476;
CC O42709; P29458: mcm4; NbExp=3; IntAct=EBI-1387246, EBI-913806;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10783164}.
CC Note=Associates with chromatin.
CC -!- DOMAIN: The zinc finger-like domain binds a zinc ion and is involved in
CC self-association. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCM10 family. {ECO:0000305}.
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DR EMBL; AJ224944; CAA12235.1; -; Genomic_DNA.
DR EMBL; AB011244; BAA24935.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB37441.1; -; Genomic_DNA.
DR PIR; T43323; T43323.
DR RefSeq; NP_596702.1; NM_001022626.2.
DR AlphaFoldDB; O42709; -.
DR SMR; O42709; -.
DR BioGRID; 276387; 53.
DR IntAct; O42709; 19.
DR MINT; O42709; -.
DR STRING; 4896.SPBC1347.10.1; -.
DR iPTMnet; O42709; -.
DR SwissPalm; O42709; -.
DR MaxQB; O42709; -.
DR PaxDb; O42709; -.
DR PRIDE; O42709; -.
DR EnsemblFungi; SPBC1347.10.1; SPBC1347.10.1:pep; SPBC1347.10.
DR GeneID; 2539838; -.
DR KEGG; spo:SPBC1347.10; -.
DR PomBase; SPBC1347.10; -.
DR VEuPathDB; FungiDB:SPBC1347.10; -.
DR eggNOG; KOG3056; Eukaryota.
DR HOGENOM; CLU_426518_0_0_1; -.
DR InParanoid; O42709; -.
DR OMA; FRYEFTE; -.
DR PhylomeDB; O42709; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR PRO; PR:O42709; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IDA:PomBase.
DR GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0003896; F:DNA primase activity; IDA:PomBase.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:1904931; F:MCM complex binding; IPI:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IMP:PomBase.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR040184; Mcm10.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR015408; Znf_Mcm10/DnaG.
DR PANTHER; PTHR13454; PTHR13454; 1.
DR Pfam; PF09329; zf-primase; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA replication; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..593
FT /note="DNA replication licensing factor mcm10"
FT /id="PRO_0000096280"
FT REGION 1..220
FT /note="Interaction with dfp1-hsk1 complex"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..593
FT /note="Interaction with mcm complex"
FT REGION 211..295
FT /note="Interaction with dfp1-hsk1 complex"
FT REGION 299..324
FT /note="Zinc finger-like"
FT REGION 452..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 586
FT /note="E->A: Lethal; no effect on primase activity."
FT /evidence="ECO:0000269|PubMed:16720577"
FT MUTAGEN 587
FT /note="D->A: Lethal; lowers primase activity 3-fold."
FT /evidence="ECO:0000269|PubMed:16720577"
FT MUTAGEN 588
FT /note="D->A: Lethal; lowers primase activity 15-fold."
FT /evidence="ECO:0000269|PubMed:16720577"
SQ SEQUENCE 593 AA; 66633 MW; AA2CDB29E74BD349 CRC64;
MHDPFIAEEN DLDLEEKRLQ RQLNEIQEKK RLRSAQKEAS SENAEVIQVP RSPPQQVRVL
TVSSPSKLKS PKRLILGIDK GKTGKDVSLG KGPRGPLPKP FHERLAEARN QERKRSDKLK
TMKKNRKQSF QRKRNILEDG KSEEEKFPMK CDEIDPYSRQ AIVIRYISDE VAKENIGGNQ
VYLIHQLLKL VRAPKFEAPE VDNYVVMGIV ASNSGTRETV NGNKYCMLTL TDLKWQLECF
LFGKAFERYW KIQSGTVIAL LNPEVLKPKN PDIGRFSLKL DSEYDVLLEI GRSKHLGYCS
SRRKSGELCK HWLDKRAGDV CEYHVDLAVQ RSMSTRTEFA SSMATMHEPR ARREKRFRGQ
GFQGYFAGEK YSAIPNAVAG LYDAEDAVQT ERERKERYKK QRAQAERERE ILVRLSKRCC
ASSSSSSNSN NLSTGMSMRT LGHQYLNLQG SGVKNLHDKG NPTALSKDSE IDSSTKKPSV
LASFNASIMN PKSSLPSFSN SAILGTNDAA SGTPVPQDTT STKVSPAVVF TSSPRIFSPQ
SLRKIGFDPT HSADASTTHS TATGLSRSGS LKNIKFRYEF TESDDEDDLE IVP
