MCM4_SCHPO
ID MCM4_SCHPO Reviewed; 931 AA.
AC P29458; Q9P7K4; Q9USM0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=DNA replication licensing factor mcm4;
DE EC=3.6.4.12;
DE AltName: Full=Cell division control protein 21;
DE AltName: Full=Minichromosome maintenance protein 4;
GN Name=mcm4; Synonyms=cdc21; ORFNames=SPCC16A11.17, SPCC24B10.01;
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=1454522; DOI=10.1093/nar/20.21.5571;
RA Coxon A., Maundrell K., Kearsey S.E.;
RT "Fission yeast cdc21+ belongs to a family of proteins involved in an early
RT step of chromosome replication.";
RL Nucleic Acids Res. 20:5571-5577(1992).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Kearsey S.E.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-38; SER-41 AND
RP SER-92, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 S phase execution. {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. {ECO:0000269|PubMed:11606526,
CC ECO:0000305}.
CC -!- INTERACTION:
CC P29458; O42709: mcm10; NbExp=3; IntAct=EBI-913806, EBI-1387246;
CC P29458; O94450: SPAC1687.04; NbExp=3; IntAct=EBI-913806, EBI-7492115;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; X58824; CAA41628.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB53089.1; -; Genomic_DNA.
DR PIR; S26640; S26640.
DR RefSeq; NP_588004.2; NM_001022995.2.
DR AlphaFoldDB; P29458; -.
DR SMR; P29458; -.
DR ComplexPortal; CPX-2945; MCM complex.
DR IntAct; P29458; 10.
DR MINT; P29458; -.
DR STRING; 4896.SPCC16A11.17.1; -.
DR iPTMnet; P29458; -.
DR MaxQB; P29458; -.
DR PaxDb; P29458; -.
DR PRIDE; P29458; -.
DR GeneID; 2539164; -.
DR KEGG; spo:SPCC16A11.17; -.
DR PomBase; SPCC16A11.17; mcm4.
DR eggNOG; KOG0478; Eukaryota.
DR HOGENOM; CLU_000995_7_1_1; -.
DR InParanoid; P29458; -.
DR PhylomeDB; P29458; -.
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:P29458; -.
DR Proteomes; UP000002485; Chromosome III.
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:0030875; C:rDNA protrusion; 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:0003682; F:chromatin binding; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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; IMP:PomBase.
DR GO; GO:0006279; P:premeiotic DNA replication; IMP:PomBase.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0048478; P:replication fork protection; IMP:PomBase.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
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:SF66; PTHR11630:SF66; 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; PR01660; MCMPROTEIN4.
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; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..931
FT /note="DNA replication licensing factor mcm4"
FT /id="PRO_0000194106"
FT DOMAIN 493..702
FT /note="MCM"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 677..680
FT /note="Arginine finger"
FT COMPBIAS 1..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 545..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 872..891
FT /note="Missing (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 931 AA; 103728 MW; BCA9B045FC62811D CRC64;
MSSSQQSGRA NELRTPGRAN SSSREAVDSS PLFFPASSPG STRLTTPRTT ARTPLASSPL
LFESSSPGPN IPQSSRSHLL SQRNDLFLDS SSQRTPRSTR RGDIHSSVQM STPSRRREVD
PQRPGVSTPS SLLFSGSDAL TFSQAHPSSE VADDTVRVIW GTNVSIQESI ASFRGFLRGF
KKKYRPEYRN ELMPPPDAEQ LVYIEALRNM RIMGLEILNL DVQDLKHYPP TKKLYHQLYS
YPQEIIPIMD QTIKDVMLDL LGTNPPEDVL NDIELKIYKI RPFNLEKCIN MRDLNPGDID
KLISIKGLVL RCTPVIPDMK QAFFRCSVCG HCVTVEIDRG RIAEPIKCPR EVCGATNAMQ
LIHNRSEFAD KQVIKLQETP DVVPDGQTPH SVSLCVYDEL VDSARAGDRI EVTGIFRCVP
VRLNPRMRTV KSLFKTYVDV VHIKKQDKRR LGTDPSTLES DIAEDAALQI DEVRKISDEE
VEKIQQVSKR DDIYDILSRS LAPSIYEMDD VKKGLLLQLF GGTNKSFHKG ASPRYRGDIN
ILMCGDPSTS KSQILKYVHK IAPRGVYTSG KGSSAVGLTA YITRDQDTKQ LVLESGALVL
SDGGICCIDE FDKMSDATRS ILHEVMEQQT VTVAKAGIIT TLNARTSILA SANPIGSKYN
PDLPVTKNID LPPTLLSRFD LVYLILDRVD ETLDRKLANH IVSMYMEDTP EHATDMEVFS
VEFLTSYITY ARNNINPVIS EEAAKELVNA YVGMRKLGED VRASEKRITA TTRQLESMIR
LSEAHAKMHL RNVVEVGDVL EAARLIKTAI KDYATDPATG KISLDLIYVN ERETLVPEDM
VKELANLISN LTVGGKTMLV SQLLTRFREQ SSTRLDASDF EACLGAFREQ SSTRLDASDF
EACLGALERR GRIKVITSAG HRIVRSIAQT D
