Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Minichromosome maintenance protein MCM

Gene

MCM

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM 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 helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.2 Publications

Enzyme regulationi

Inhibited by the cdc6-2 protein. The ATPase activity is not stimulated in the presence of DNA molecules.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi340 – 3478ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

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

BioCyciSSOL273057:GCH2-743-MONOMER.
BRENDAi3.6.4.12. 6163.

Names & Taxonomyi

Protein namesi
Recommended name:
Minichromosome maintenance protein MCM (EC:3.6.4.12)
Gene namesi
Name:MCM
Ordered Locus Names:SSO0774
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi189 – 1891L → D: Predominanatly monomeric and loss of helicase activity; when associated with R-191. 1 Publication
Mutagenesisi191 – 1911D → R: Predominanatly monomeric and loss of helicase activity; when associated with D-189. 1 Publication
Mutagenesisi202 – 2043EEV → GGG: Loss of helicase activity. 1 Publication
Mutagenesisi318 – 3181F → A: No effect on helicase and ATPase activity. 1 Publication
Mutagenesisi326 – 3272ED → AA: Impairs helicase activity; when associated with A-329. 1 Publication
Mutagenesisi329 – 3291R → A: Impairs helicase activity; when associated with 326-A-A-327. 1 Publication
Mutagenesisi331 – 3311R → A: Loss of helicase and ATPase activity. 1 Publication
Mutagenesisi346 – 3461K → A: Loss of helicase and ATPase activity. 2 Publications
Mutagenesisi346 – 3461K → A: Sharp decrease in ATPase activity. Almost devoid of helicase activity. 2 Publications
Mutagenesisi359 – 3591R → A: Loss of helicase and reduction of ATPase activity. 1 Publication
Mutagenesisi366 – 3661K → E: Loss of helicase and reduction of ATPase activity. 1 Publication
Mutagenesisi374 – 3741T → E: Reduction of helicase and gain of ATPase activity. 1 Publication
Mutagenesisi404 – 4041D → A: Loss of helicase and ATPase activity. 1 Publication
Mutagenesisi416 – 4161A → R: Predominanatly monomeric and loss of helicase activity; when associated with R-420. 1 Publication
Mutagenesisi420 – 4201A → R: Predominanatly monomeric and loss of helicase activity; when associated with R-416. 1 Publication
Mutagenesisi423 – 4242QQ → AA: Loss of helicase and ATPase activity. 1 Publication
Mutagenesisi448 – 4481N → A: Loss of helicase and ATPase activity. 1 Publication
Mutagenesisi473 – 4731R → A: Loss of helicase and ATPase activity. 1 Publication
Mutagenesisi488 – 4881D → A: No effect on helicase and reduction of ATPase activity. 1 Publication
Mutagenesisi550 – 5545TPDSP → GGGGG: Predominanatly monomeric and loss of helicase activity. 1 Publication
Mutagenesisi555 – 5573ILI → DSD: Exclusively monomeric and loss of helicase activity, ATPase activity and DNA binding. 1 Publication
Mutagenesisi560 – 5601R → A: Loss of helicase and ATPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 686686Minichromosome maintenance protein MCMPRO_0000194128Add
BLAST

Interactioni

Subunit structurei

Homohexamers. Forms a complex with SSB.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ORF-c40_009Q9UXG05EBI-8081298,EBI-8081318From a different organism.

Protein-protein interaction databases

DIPiDIP-42884N.
IntActiQ9UXG1. 1 interaction.
MINTiMINT-1896063.
STRINGi273057.SSO0774.

Structurei

Secondary structure

1
686
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2011Combined sources
Beta strandi24 – 274Combined sources
Helixi29 – 3911Combined sources
Beta strandi43 – 486Combined sources
Helixi49 – 557Combined sources
Helixi57 – 659Combined sources
Helixi67 – 8519Combined sources
Helixi89 – 924Combined sources
Beta strandi97 – 1026Combined sources
Helixi109 – 1113Combined sources
Helixi114 – 1163Combined sources
Beta strandi119 – 13012Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi141 – 1455Combined sources
Turni147 – 1493Combined sources
Beta strandi152 – 1565Combined sources
Turni172 – 1743Combined sources
Beta strandi179 – 1824Combined sources
Helixi184 – 1863Combined sources
Beta strandi187 – 19812Combined sources
Helixi201 – 2033Combined sources
Beta strandi212 – 2187Combined sources
Helixi219 – 2213Combined sources
Beta strandi230 – 24011Combined sources
Beta strandi251 – 26414Combined sources
Helixi612 – 6154Combined sources
Helixi621 – 63717Combined sources
Beta strandi640 – 6445Combined sources
Helixi645 – 65511Combined sources
Helixi659 – 67214Combined sources
Beta strandi674 – 6796Combined sources
Beta strandi682 – 6854Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M45NMR-A605-686[»]
2VL6X-ray2.80A/B/C1-268[»]
3F9VX-ray4.35A7-601[»]
4FDGX-ray4.10A/B/C/D/E7-686[»]
4R7YX-ray2.70A/B2-269[»]
ProteinModelPortaliQ9UXG1.
SMRiQ9UXG1. Positions 7-265.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UXG1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini291 – 495205MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi472 – 4754Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG00439. Archaea.
COG1241. LUCA.
HOGENOMiHOG000224127.
InParanoidiQ9UXG1.
KOiK10726.
OMAiQYIDWQK.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
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.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UXG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIPSKQIDY RDVFIEFLTT FKGNNNQNKY IERINELVAY RKKSLIIEFS
60 70 80 90 100
DVLSFNENLA YEIINNTKII LPILEGALYD HILQLDPTYQ RDIEKVHVRI
110 120 130 140 150
VGIPRVIELR KIRSTDIGKL ITIDGILVKV TPVKERIYKA TYKHIHPDCM
160 170 180 190 200
QEFEWPEDEE MPEVLEMPTI CPKCGKPGQF RLIPEKTKLI DWQKAVIQER
210 220 230 240 250
PEEVPSGQLP RQLEIILEDD LVDSARPGDR VKVTGILDIK QDSPVKRGSR
260 270 280 290 300
AVFDIYMKVS SIEVSQKVLD EVIISEEDEK KIKDLAKDPW IRDRIISSIA
310 320 330 340 350
PSIYGHWELK EALALALFGG VPKVLEDTRI RGDIHILIIG DPGTAKSQML
360 370 380 390 400
QFISRVAPRA VYTTGKGSTA AGLTAAVVRE KGTGEYYLEA GALVLADGGI
410 420 430 440 450
AVIDEIDKMR DEDRVAIHEA MEQQTVSIAK AGIVAKLNAR AAVIAAGNPK
460 470 480 490 500
FGRYISERPV SDNINLPPTI LSRFDLIFIL KDQPGEQDRE LANYILDVHS
510 520 530 540 550
GKSTKNIIDI DTLRKYIAYA RKYVTPKITS EAKNLITDFF VEMRKKSSET
560 570 580 590 600
PDSPILITPR QLEALIRISE AYAKMALKAE VTREDAERAI NIMRLFLESV
610 620 630 640 650
GVDMESGKID IDTIMTGKPK SAREKMMKII EIIDSLAVSS ECAKVKDILK
660 670 680
EAQQVGIEKS NIEKLLTDMR KSGIIYEAKP ECYKKV
Length:686
Mass (Da):77,428
Last modified:May 1, 2000 - v1
Checksum:iC3ECD380F272E77E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18930 Genomic DNA. Translation: CAB57529.1.
AE006641 Genomic DNA. Translation: AAK41071.1.
PIRiH90226.
RefSeqiWP_009991364.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK41071; AAK41071; SSO0774.
GeneIDi27427101.
KEGGisso:SSO0774.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18930 Genomic DNA. Translation: CAB57529.1.
AE006641 Genomic DNA. Translation: AAK41071.1.
PIRiH90226.
RefSeqiWP_009991364.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M45NMR-A605-686[»]
2VL6X-ray2.80A/B/C1-268[»]
3F9VX-ray4.35A7-601[»]
4FDGX-ray4.10A/B/C/D/E7-686[»]
4R7YX-ray2.70A/B2-269[»]
ProteinModelPortaliQ9UXG1.
SMRiQ9UXG1. Positions 7-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42884N.
IntActiQ9UXG1. 1 interaction.
MINTiMINT-1896063.
STRINGi273057.SSO0774.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK41071; AAK41071; SSO0774.
GeneIDi27427101.
KEGGisso:SSO0774.

Phylogenomic databases

eggNOGiarCOG00439. Archaea.
COG1241. LUCA.
HOGENOMiHOG000224127.
InParanoidiQ9UXG1.
KOiK10726.
OMAiQYIDWQK.

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-743-MONOMER.
BRENDAi3.6.4.12. 6163.

Miscellaneous databases

EvolutionaryTraceiQ9UXG1.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
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.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "Physical and functional interaction between the mini-chromosome maintenance-like DNA helicase and the single-stranded DNA binding protein from the crenarchaeon Sulfolobus solfataricus."
    Carpentieri F., De Felice M., De Falco M., Rossi M., Pisani F.M.
    J. Biol. Chem. 277:12118-12127(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-346.
  4. "ATPase site architecture and helicase mechanism of an archaeal MCM."
    Moreau M.J., McGeoch A.T., Lowe A.R., Itzhaki L.S., Bell S.D.
    Mol. Cell 28:304-314(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-318; ARG-331; LYS-346; ARG-359; LYS-366; THR-374; ASP-404; 423-GLN-GLN-424; ASN-448; ARG-473; ASP-488 AND ARG-560.
  5. "Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain."
    Liu W., Pucci B., Rossi M., Pisani F.M., Ladenstein R.
    Nucleic Acids Res. 36:3235-3243(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-268, SUBUNIT.
  6. "Crystal structure of a near-full-length archaeal MCM: functional insights for an AAA+ hexameric helicase."
    Brewster A.S., Wang G., Yu X., Greenleaf W.B., Carazo J.M., Tjajadia M., Klein M.G., Chen X.S.
    Proc. Natl. Acad. Sci. U.S.A. 105:20191-20196(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.35 ANGSTROMS) OF 7-601, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF LEU-189; ASP-191; 202-GLU--VAL-204; 326-GLU-ASP-327; ARG-329; ALA-416; ALA-420; 550-THR--PRO-554 AND 555-ILE--ASP-557.

Entry informationi

Entry nameiMCM_SULSO
AccessioniPrimary (citable) accession number: Q9UXG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.