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Protein

DNA replication licensing factor mcm6

Gene

mcm6

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).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi476 – 4838ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • DNA duplex unwinding Source: GOC
  • double-strand break repair via homologous recombination Source: PomBase
  • mitotic DNA replication Source: PomBase
  • mitotic DNA replication initiation Source: PomBase
  • premeiotic DNA replication 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 mcm6 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance protein 6
Gene namesi
Name:mcm6
Synonyms:mis5
ORF Names:SPBC211.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC211.04c.
PomBaseiSPBC211.04c. mcm6.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • 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 – 892892DNA replication licensing factor mcm6PRO_0000194118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961Phosphoserine1 Publication
Modified residuei98 – 981Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49731.

PTM databases

iPTMnetiP49731.

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.Curated2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SPAC1687.04O944502EBI-913838,EBI-7492115

Protein-protein interaction databases

BioGridi277303. 25 interactions.
IntActiP49731. 9 interactions.
MINTiMINT-4690514.

Structurei

3D structure databases

ProteinModelPortaliP49731.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini426 – 633208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi608 – 6114Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000224130.
InParanoidiP49731.
KOiK02542.
OMAiIDMENNG.
OrthoDBiEOG7Z69MX.
PhylomeDBiP49731.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PANTHERiPTHR11630:SF43. PTHR11630:SF43. 4 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
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.

P49731-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLASQGNN ASTPAYRYGF QTSEVGDRPT VSMPSQPESS AMLEDDGMVK
60 70 80 90 100
RKPFAAIGEA IPKVIDTTGE SVREAFEEFL LSFSDDRVAG GDALPSASQE
110 120 130 140 150
KYYVQQIHGL AMYEIHTVYV DYKHLTSYND VLALAIVEQY YRFSPFLLRA
160 170 180 190 200
LQKLIEKFEP EYYRSSLSRE NASLSPNFKA SDKTFALAFY NLPFRSTIRD
210 220 230 240 250
LRTDRIGRLT TITGTVTRTS EVRPELAQGT FICEECHTVV SNVEQAFRYT
260 270 280 290 300
EPTQCPNELC ANKRSWRLNI SQSSFQDWQK VRIQENSNEI PTGSMPRTLD
310 320 330 340 350
VILRGDIVER AKAGDKCAFT GILIAVPDVS QLGIPGVKPE AYRDSRNFGG
360 370 380 390 400
RDADGVTGLK SLGVRDLTYK LSFLACMVQP DDANDKSGAD VRGDGSQGIE
410 420 430 440 450
EQDEFLQSLS QEEIDDLRAM VHSDHIYSRL TNSLAPSVYG HEIIKKGILL
460 470 480 490 500
QLMGGVHKLT PEGINLRGDL NICIVGDPST SKSQFLKYVC NFLPRAIYTS
510 520 530 540 550
GKASSAAGLT AAVVKDEETG DFTIEAGALM LADNGICAID EFDKMDLSDQ
560 570 580 590 600
VAIHEAMEQQ TISIAKAGIQ ATLNARTSIL AAANPIGGRY NRKTTLRNNI
610 620 630 640 650
NMSAPIMSRF DLFFVVLDEC NESVDRHLAK HIVDIHRLRD DAMQPEFSTE
660 670 680 690 700
QLQRYIRYAR TFKPKLNTES CAEIVKKYKQ LRMDDAQGAG KNSYRITVRQ
710 720 730 740 750
LESMIRLSEA IARANCVDDI TPAFVNEAYS LLRQSIIHVE RDDIEVEEDD
760 770 780 790 800
AEAQELENDN TNTTNGNDNV SSEEALQKPK VKITYDKYVS IMNGILQVLR
810 820 830 840 850
QRSTEGVDGV PAGDLVQSYL ELREDQFHTE EDIIYEVGLV RKVLTRLVHE
860 870 880 890
SIIMEIQNLT DSAVRLPFEE RVFSIHPNCD IDALLSNGDV PN
Length:892
Mass (Da):99,550
Last modified:August 14, 2001 - v2
Checksum:i3A00DB55B2EE08B7
GO

Sequence cautioni

The sequence BAA06729.1 differs from that shown. Reason: Frameshift at position 864. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31960 Genomic DNA. Translation: BAA06729.1. Frameshift.
CU329671 Genomic DNA. Translation: CAB75412.1.
PIRiT43423.
T50339.
RefSeqiNP_596614.1. NM_001022535.2.

Genome annotation databases

EnsemblFungiiSPBC211.04c.1; SPBC211.04c.1:pep; SPBC211.04c.
GeneIDi2540784.
KEGGispo:SPBC211.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31960 Genomic DNA. Translation: BAA06729.1. Frameshift.
CU329671 Genomic DNA. Translation: CAB75412.1.
PIRiT43423.
T50339.
RefSeqiNP_596614.1. NM_001022535.2.

3D structure databases

ProteinModelPortaliP49731.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277303. 25 interactions.
IntActiP49731. 9 interactions.
MINTiMINT-4690514.

PTM databases

iPTMnetiP49731.

Proteomic databases

MaxQBiP49731.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC211.04c.1; SPBC211.04c.1:pep; SPBC211.04c.
GeneIDi2540784.
KEGGispo:SPBC211.04c.

Organism-specific databases

EuPathDBiFungiDB:SPBC211.04c.
PomBaseiSPBC211.04c. mcm6.

Phylogenomic databases

HOGENOMiHOG000224130.
InParanoidiP49731.
KOiK02542.
OMAiIDMENNG.
OrthoDBiEOG7Z69MX.
PhylomeDBiP49731.

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

NextBioi20801902.
PROiP49731.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008049. MCM6.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PANTHERiPTHR11630:SF43. PTHR11630:SF43. 4 hits.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01662. MCMPROTEIN6.
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 minichromosome loss mutants mis cause lethal aneuploidy and replication abnormality."
    Takahashi K., Yamada H., Yanagida M.
    Mol. Biol. Cell 5:1145-1158(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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. "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.
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-98, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMCM6_SCHPO
AccessioniPrimary (citable) accession number: P49731
Secondary accession number(s): Q9P7R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 14, 2001
Last modified: April 13, 2016
This is version 134 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.