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Protein

DNA replication licensing factor mcm5

Gene

mcm5

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). Role in DNA replication and essential for viability.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi372 – 3798ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • DNA duplex unwinding Source: GOC
  • mitotic DNA replication initiation Source: PomBase
  • negative regulation of helicase activity 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 mcm5 (EC:3.6.4.12)
Alternative name(s):
Cell division control protein nda4
Minichromosome maintenance protein 5
Gene namesi
Name:mcm5
Synonyms:nda4
ORF Names:SPAC1B2.05, SPAC3F10.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC1B2.05. mcm5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • DNA replication preinitiation complex Source: PomBase
  • MCM complex 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 – 720720DNA replication licensing factor mcm5PRO_0000194112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei350 – 3501Phosphoserine1 Publication
Modified residuei352 – 3521Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41389.
PRIDEiP41389.

PTM databases

iPTMnetiP41389.

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).Curated1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SPAC1687.04O944502EBI-913821,EBI-7492115

Protein-protein interaction databases

IntActiP41389. 3 interactions.
MINTiMINT-4690032.

Structurei

3D structure databases

ProteinModelPortaliP41389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini322 – 529208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi504 – 5074Arginine finger

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi307 – 3126Poly-Glu

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000224128.
InParanoidiP41389.
OrthoDBiEOG7B5X4C.
PhylomeDBiP41389.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008048. MCM5.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01661. MCMPROTEIN5.
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.

P41389-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATGWERS AVYYTPVLPG EQELDSNVSH EKNFIQFIEE FVIDNDFIYR
60 70 80 90 100
TQLRDNLVVK QYMLNIDLRH LISYNEDLAH LLLSQPTDIL PLFESAVTTV
110 120 130 140 150
AKRLLYRSQE NASTNIPTCQ VTLRYDANIL PIRNLTASHI SKLVRVPGII
160 170 180 190 200
IGASTLSCRA TALHLVCRNC RATRILQISG GFSGVQLPRV CEAPVLDGEK
210 220 230 240 250
KDCPMDPFII DHSKSTFIDQ QVLKLQEAPD MVPVGELPRH ILLNADRYLT
260 270 280 290 300
NQITPGTRCV ITGIFSIFQN KSVKASGAVA IRNPYIRVVG IQMDSNDGSK
310 320 330 340 350
STPLFSEEEE EEFLEISRTP NLYDIISNSI SPAIYGNVDI KKAIACLLFS
360 370 380 390 400
GSKKILPDGM RLRGDINVLL LGDPGTAKSQ FLKFVERLAP IAVYTSGKGS
410 420 430 440 450
SAAGLTASIQ RDSVTREFYL EGGAMVLADG GIVCIDEFDK MRDEDRVAIH
460 470 480 490 500
EAMEQQTISI AKAGITTILN SRTSVLAAAN PIFGRYDDMK TPGENIDFQS
510 520 530 540 550
TILSRFDMIF IVKDEHDETK DRNIARHVIN LHTNLQESSE TLAIGEIPFD
560 570 580 590 600
KFRRYINYCR HKCAPNLDAE AAEKLSSQFV AIRKLVHQSE QDSNSRSTIP
610 620 630 640 650
ITVRQLEAII RITESLAKMS LSPIASEAHA TEAIRLFLTS TLAAATQSSP
660 670 680 690 700
EVTEEVKKIE ASLRKRLPIG FQASYRMLIR EYVNGHGYSQ HALEMALQIR
710 720
SSKETIQLRN GGQTVYRSGV
Length:720
Mass (Da):80,100
Last modified:October 1, 1996 - v2
Checksum:i52F3EA9DD127E56E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti461 – 4611A → R in AAC60568 (PubMed:8298187).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S68467 Genomic DNA. Translation: AAC60568.1.
CU329670 Genomic DNA. Translation: CAB61472.1.
PIRiA48723.
T50141.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S68467 Genomic DNA. Translation: AAC60568.1.
CU329670 Genomic DNA. Translation: CAB61472.1.
PIRiA48723.
T50141.

3D structure databases

ProteinModelPortaliP41389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP41389. 3 interactions.
MINTiMINT-4690032.

PTM databases

iPTMnetiP41389.

Proteomic databases

MaxQBiP41389.
PRIDEiP41389.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

PomBaseiSPAC1B2.05. mcm5.

Phylogenomic databases

HOGENOMiHOG000224128.
InParanoidiP41389.
OrthoDBiEOG7B5X4C.
PhylomeDBiP41389.

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

PROiP41389.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008048. MCM5.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01661. MCMPROTEIN5.
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 genes nda1+ and nda4+, mutations of which lead to S-phase block, chromatin alteration and Ca2+ suppression, are members of the CDC46/MCM2 family."
    Miyake S., Okishio N., Samejima I., Hiraoka Y., Toda T., Saitoh I., Yanagida M.
    Mol. Biol. Cell 4:1003-1015(1993) [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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMCM5_SCHPO
AccessioniPrimary (citable) accession number: P41389
Secondary accession number(s): Q9UTF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 133 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.