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Protein

DNA replication licensing factor mcm7

Gene

mcm7

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 the progression of S phase.By similarity1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi403 – 4108ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • DNA duplex unwinding Source: GOC
  • mitotic DNA replication initiation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, 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 mcm7 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance protein 7
Gene namesi
Name:mcm7
ORF Names:SPBC25D12.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC25D12.03c.
PomBaseiSPBC25D12.03c. mcm7.

Subcellular locationi

  • Nucleus 1 Publication

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
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 760760DNA replication licensing factor mcm7PRO_0000194123Add
BLAST

Proteomic databases

MaxQBiO75001.
PRIDEiO75001.

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. Interacts with sld3 and mcm10.Curated3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SPAC1687.04O944502EBI-913851,EBI-7492115

Protein-protein interaction databases

BioGridi277156. 16 interactions.
IntActiO75001. 5 interactions.
MINTiMINT-4783150.

Structurei

3D structure databases

ProteinModelPortaliO75001.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini353 – 559207MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi535 – 5384Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000224125.
InParanoidiO75001.
KOiK02210.
OMAiQTRACRF.
OrthoDBiEOG7Z69MX.
PhylomeDBiO75001.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008050. MCM7.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF26. PTHR11630:SF26. 3 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01663. MCMPROTEIN7.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75001-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPTIDLKI PEYEECQHKI TDFLSHFKQE QVQDGQQNQD ISMSDAGDEP
60 70 80 90 100
FLKSKYMDIL QKISNRESNV INVDLNDLYE FDPSDTQLLH NIESNAKRFV
110 120 130 140 150
ELFSQCADAL MPPPTVEINY RNEVLDVIMQ QRVQRNENID PEHKGFPPEL
160 170 180 190 200
TRGYDLYFRP VTRNKKPFSV RDLRGENLGS LLTVRGIVTR TSDVKPSLTV
210 220 230 240 250
NAYTCDRCGY EVFQEIRQKT FLPMSECPSD ECKKNDAKGQ LFMSTRASKF
260 270 280 290 300
LPFQEVKIQE LTNQVPIGHI PRSLTVHLYG AITRSVNPGD IVDISGIFLP
310 320 330 340 350
TPYTGFRAMR AGLLTDTYLE CHYVSQIIKN YTNIEKTPQS EAAIAELNQG
360 370 380 390 400
GNVYEKLAKS IAPEIYGHED VKKALLLLLV GGVTKELGDG MRIRGDINIC
410 420 430 440 450
LTGDPGVAKS QLLKYISKVA PRGVYTTGRG SSGVGLTAAV MRDPVTDEMV
460 470 480 490 500
LEGGALVLAD NGICCIDEFD KMDESDRTAI HEVMEQQTIS ISKAGITTTL
510 520 530 540 550
NARTSILAAA NPLYGRYNPK VAPIHNINLP AALLSRFDIL FLILDTPSRE
560 570 580 590 600
TDEHLAQHVT YVHMHNEQPK MDFEPLDPNM IRHYISSARQ YRPVVPKDVC
610 620 630 640 650
DYVTGAYVQL RQNQKRDEAN ERQFAHTTPR TLLAILRMGQ ALARLRFSNR
660 670 680 690 700
VEIGDVDEAL RLMSVSKSSL YDDLDPSSHD TTITSKIYKI IRDMLNSIPD
710 720 730 740 750
VEGNERSLTL RAIRERVLAK GFTEDHLINT IQEYTDLGVL LTTNNGQTIM
760
FLDPDLHMEN
Length:760
Mass (Da):85,622
Last modified:November 1, 1998 - v1
Checksum:i2141F8F9CB0BAA34
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti457 – 4571V → I in CAA03898 (PubMed:9366552).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070481 Genomic DNA. Translation: AAC23693.1.
CU329671 Genomic DNA. Translation: CAA20099.1.
AJ000065 Genomic DNA. Translation: CAA03898.1.
PIRiT39991.
RefSeqiNP_596545.1. NM_001022466.2.

Genome annotation databases

EnsemblFungiiSPBC25D12.03c.1; SPBC25D12.03c.1:pep; SPBC25D12.03c.
GeneIDi2540630.
KEGGispo:SPBC25D12.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070481 Genomic DNA. Translation: AAC23693.1.
CU329671 Genomic DNA. Translation: CAA20099.1.
AJ000065 Genomic DNA. Translation: CAA03898.1.
PIRiT39991.
RefSeqiNP_596545.1. NM_001022466.2.

3D structure databases

ProteinModelPortaliO75001.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277156. 16 interactions.
IntActiO75001. 5 interactions.
MINTiMINT-4783150.

Proteomic databases

MaxQBiO75001.
PRIDEiO75001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC25D12.03c.1; SPBC25D12.03c.1:pep; SPBC25D12.03c.
GeneIDi2540630.
KEGGispo:SPBC25D12.03c.

Organism-specific databases

EuPathDBiFungiDB:SPBC25D12.03c.
PomBaseiSPBC25D12.03c. mcm7.

Phylogenomic databases

HOGENOMiHOG000224125.
InParanoidiO75001.
KOiK02210.
OMAiQTRACRF.
OrthoDBiEOG7Z69MX.
PhylomeDBiO75001.

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

NextBioi20801755.
PROiO75001.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR008050. MCM7.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF26. PTHR11630:SF26. 3 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01663. MCMPROTEIN7.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: SP011.
  2. "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.
  3. "A globular complex formation by Nda1 and the other five members of the MCM protein family in fission yeast."
    Adachi Y., Usukura J., Yanagida M.
    Genes Cells 2:467-479(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 367-466.
    Strain: 972 / ATCC 24843.
  4. "SpSld3 is required for loading and maintenance of SpCdc45 on chromatin in DNA replication in fission yeast."
    Nakajima R., Masukata H.
    Mol. Biol. Cell 13:1462-1472(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLD3.
  5. "The Cdc23 (Mcm10) protein is required for the phosphorylation of minichromosome maintenance complex by the Dfp1-Hsk1 kinase."
    Lee J.-K., Seo Y.-S., Hurwitz J.
    Proc. Natl. Acad. Sci. U.S.A. 100:2334-2339(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCM10.

Entry informationi

Entry nameiMCM7_SCHPO
AccessioniPrimary (citable) accession number: O75001
Secondary accession number(s): P87302
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: April 13, 2016
This is version 131 of the entry and version 1 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.