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Protein

DNA replication licensing factor mcm4

Gene

mcm4

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Required for S phase execution.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi545 – 5528ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: PomBase
  • DNA binding Source: UniProtKB-KW
  • DNA helicase activity Source: InterPro

GO - Biological processi

  • DNA duplex unwinding Source: GOC
  • mitotic DNA replication initiation Source: PomBase
  • negative regulation of ATP-dependent DNA helicase activity Source: PomBase
  • premeiotic DNA replication Source: PomBase
  • replication fork protection Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-68962. Activation of the pre-replicative complex.
R-SPO-69052. Switching of origins to a post-replicative state.
R-SPO-69300. Removal of licensing factors from origins.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor mcm4 (EC:3.6.4.12)
Alternative name(s):
Cell division control protein 21
Minichromosome maintenance protein 4
Gene namesi
Name:mcm4
Synonyms:cdc21
ORF Names:SPCC16A11.17, SPCC24B10.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

PomBaseiSPCC16A11.17. mcm4.

Subcellular locationi

GO - Cellular componenti

  • DNA replication preinitiation complex Source: PomBase
  • MCM complex Source: PomBase
  • MCM core complex Source: PomBase
  • nuclear chromatin Source: PomBase
  • nuclear pre-replicative complex Source: PomBase
  • nuclear replication fork Source: PomBase
  • nucleus Source: PomBase
  • rDNA protrusion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 931931DNA replication licensing factor mcm4PRO_0000194106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371Phosphoserine1 Publication
Modified residuei38 – 381Phosphoserine1 Publication
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei92 – 921Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29458.

PTM databases

iPTMnetiP29458.

Interactioni

Subunit structurei

Component of the mcm2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-mcm7-mcm3-mcm5 (Probable). The heterodimers of mcm4/mcm6 and mcm3/mcm5 interact with mcm2 and mcm7.Curated1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
mcm10O427093EBI-913806,EBI-1387246
SPAC1687.04O944503EBI-913806,EBI-7492115

Protein-protein interaction databases

IntActiP29458. 10 interactions.
MINTiMINT-1897411.

Structurei

3D structure databases

ProteinModelPortaliP29458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini493 – 702210MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi677 – 6804Arginine finger

Sequence similaritiesi

Belongs to the MCM family.Curated
Contains 1 MCM domain.Curated

Phylogenomic databases

HOGENOMiHOG000224127.
InParanoidiP29458.
OrthoDBiEOG7B5X4C.
PhylomeDBiP29458.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008047. MCM_4.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01660. MCMPROTEIN4.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29458-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSQQSGRA NELRTPGRAN SSSREAVDSS PLFFPASSPG STRLTTPRTT
60 70 80 90 100
ARTPLASSPL LFESSSPGPN IPQSSRSHLL SQRNDLFLDS SSQRTPRSTR
110 120 130 140 150
RGDIHSSVQM STPSRRREVD PQRPGVSTPS SLLFSGSDAL TFSQAHPSSE
160 170 180 190 200
VADDTVRVIW GTNVSIQESI ASFRGFLRGF KKKYRPEYRN ELMPPPDAEQ
210 220 230 240 250
LVYIEALRNM RIMGLEILNL DVQDLKHYPP TKKLYHQLYS YPQEIIPIMD
260 270 280 290 300
QTIKDVMLDL LGTNPPEDVL NDIELKIYKI RPFNLEKCIN MRDLNPGDID
310 320 330 340 350
KLISIKGLVL RCTPVIPDMK QAFFRCSVCG HCVTVEIDRG RIAEPIKCPR
360 370 380 390 400
EVCGATNAMQ LIHNRSEFAD KQVIKLQETP DVVPDGQTPH SVSLCVYDEL
410 420 430 440 450
VDSARAGDRI EVTGIFRCVP VRLNPRMRTV KSLFKTYVDV VHIKKQDKRR
460 470 480 490 500
LGTDPSTLES DIAEDAALQI DEVRKISDEE VEKIQQVSKR DDIYDILSRS
510 520 530 540 550
LAPSIYEMDD VKKGLLLQLF GGTNKSFHKG ASPRYRGDIN ILMCGDPSTS
560 570 580 590 600
KSQILKYVHK IAPRGVYTSG KGSSAVGLTA YITRDQDTKQ LVLESGALVL
610 620 630 640 650
SDGGICCIDE FDKMSDATRS ILHEVMEQQT VTVAKAGIIT TLNARTSILA
660 670 680 690 700
SANPIGSKYN PDLPVTKNID LPPTLLSRFD LVYLILDRVD ETLDRKLANH
710 720 730 740 750
IVSMYMEDTP EHATDMEVFS VEFLTSYITY ARNNINPVIS EEAAKELVNA
760 770 780 790 800
YVGMRKLGED VRASEKRITA TTRQLESMIR LSEAHAKMHL RNVVEVGDVL
810 820 830 840 850
EAARLIKTAI KDYATDPATG KISLDLIYVN ERETLVPEDM VKELANLISN
860 870 880 890 900
LTVGGKTMLV SQLLTRFREQ SSTRLDASDF EACLGAFREQ SSTRLDASDF
910 920 930
EACLGALERR GRIKVITSAG HRIVRSIAQT D
Length:931
Mass (Da):103,728
Last modified:May 30, 2000 - v2
Checksum:iBCA9B045FC62811D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti872 – 89120Missing (PubMed:11859360).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58824 Genomic DNA. Translation: CAA41628.1.
CU329672 Genomic DNA. Translation: CAB53089.1.
PIRiS26640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58824 Genomic DNA. Translation: CAA41628.1.
CU329672 Genomic DNA. Translation: CAB53089.1.
PIRiS26640.

3D structure databases

ProteinModelPortaliP29458.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP29458. 10 interactions.
MINTiMINT-1897411.

PTM databases

iPTMnetiP29458.

Proteomic databases

MaxQBiP29458.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

PomBaseiSPCC16A11.17. mcm4.

Phylogenomic databases

HOGENOMiHOG000224127.
InParanoidiP29458.
OrthoDBiEOG7B5X4C.
PhylomeDBiP29458.

Enzyme and pathway databases

ReactomeiR-SPO-68962. Activation of the pre-replicative complex.
R-SPO-69052. Switching of origins to a post-replicative state.
R-SPO-69300. Removal of licensing factors from origins.

Miscellaneous databases

NextBioi20800335.
PROiP29458.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008047. MCM_4.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01660. MCMPROTEIN4.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Fission yeast cdc21+ belongs to a family of proteins involved in an early step of chromosome replication."
    Coxon A., Maundrell K., Kearsey S.E.
    Nucleic Acids Res. 20:5571-5577(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Kearsey S.E.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  4. "Characterization of Schizosaccharomyces pombe mcm7(+) and cdc23(+) (MCM10) and interactions with replication checkpoints."
    Liang D.T., Forsburg S.L.
    Genetics 159:471-486(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
    Strain: SP011.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-38; SER-41 AND SER-92, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMCM4_SCHPO
AccessioniPrimary (citable) accession number: P29458
Secondary accession number(s): Q9P7K4, Q9USM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: May 11, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.