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)DescriptionActionsGraphical viewLength
Nucleotide bindingi340 – 347ATPSequence analysis8

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi189L → D: Predominanatly monomeric and loss of helicase activity; when associated with R-191. 1 Publication1
Mutagenesisi191D → R: Predominanatly monomeric and loss of helicase activity; when associated with D-189. 1 Publication1
Mutagenesisi202 – 204EEV → GGG: Loss of helicase activity. 1 Publication3
Mutagenesisi318F → A: No effect on helicase and ATPase activity. 1 Publication1
Mutagenesisi326 – 327ED → AA: Impairs helicase activity; when associated with A-329. 1 Publication2
Mutagenesisi329R → A: Impairs helicase activity; when associated with 326-A-A-327. 1 Publication1
Mutagenesisi331R → A: Loss of helicase and ATPase activity. 1 Publication1
Mutagenesisi346K → A: Loss of helicase and ATPase activity. 2 Publications1
Mutagenesisi346K → A: Sharp decrease in ATPase activity. Almost devoid of helicase activity. 2 Publications1
Mutagenesisi359R → A: Loss of helicase and reduction of ATPase activity. 1 Publication1
Mutagenesisi366K → E: Loss of helicase and reduction of ATPase activity. 1 Publication1
Mutagenesisi374T → E: Reduction of helicase and gain of ATPase activity. 1 Publication1
Mutagenesisi404D → A: Loss of helicase and ATPase activity. 1 Publication1
Mutagenesisi416A → R: Predominanatly monomeric and loss of helicase activity; when associated with R-420. 1 Publication1
Mutagenesisi420A → R: Predominanatly monomeric and loss of helicase activity; when associated with R-416. 1 Publication1
Mutagenesisi423 – 424QQ → AA: Loss of helicase and ATPase activity. 1 Publication2
Mutagenesisi448N → A: Loss of helicase and ATPase activity. 1 Publication1
Mutagenesisi473R → A: Loss of helicase and ATPase activity. 1 Publication1
Mutagenesisi488D → A: No effect on helicase and reduction of ATPase activity. 1 Publication1
Mutagenesisi550 – 554TPDSP → GGGGG: Predominanatly monomeric and loss of helicase activity. 1 Publication5
Mutagenesisi555 – 557ILI → DSD: Exclusively monomeric and loss of helicase activity, ATPase activity and DNA binding. 1 Publication3
Mutagenesisi560R → A: Loss of helicase and ATPase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001941281 – 686Minichromosome maintenance protein MCMAdd BLAST686

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 interactor.
MINTiMINT-1896063.
STRINGi273057.SSO0774.

Structurei

Secondary structure

1686
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 20Combined sources11
Beta strandi24 – 27Combined sources4
Helixi29 – 39Combined sources11
Beta strandi43 – 48Combined sources6
Helixi49 – 55Combined sources7
Helixi57 – 65Combined sources9
Helixi67 – 85Combined sources19
Helixi89 – 92Combined sources4
Beta strandi97 – 102Combined sources6
Helixi109 – 111Combined sources3
Helixi114 – 116Combined sources3
Beta strandi119 – 130Combined sources12
Beta strandi134 – 139Combined sources6
Beta strandi141 – 145Combined sources5
Turni147 – 149Combined sources3
Beta strandi152 – 156Combined sources5
Turni172 – 174Combined sources3
Beta strandi179 – 182Combined sources4
Helixi184 – 186Combined sources3
Beta strandi187 – 198Combined sources12
Helixi201 – 203Combined sources3
Beta strandi212 – 218Combined sources7
Helixi219 – 221Combined sources3
Beta strandi230 – 240Combined sources11
Beta strandi251 – 264Combined sources14
Helixi612 – 615Combined sources4
Helixi621 – 637Combined sources17
Beta strandi640 – 644Combined sources5
Helixi645 – 655Combined sources11
Helixi659 – 672Combined sources14
Beta strandi674 – 679Combined sources6
Beta strandi682 – 685Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UXG1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini291 – 495MCMAdd BLAST205

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi472 – 475Arginine finger4

Sequence similaritiesi

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

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
PF17207. MCM_OB. 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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42884N.
IntActiQ9UXG1. 1 interactor.
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.
OMAiKHAVANN.

Enzyme and pathway databases

BRENDAi3.6.4.12. 6163.

Miscellaneous databases

EvolutionaryTraceiQ9UXG1.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR031327. MCM.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
PF17207. MCM_OB. 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...

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: November 30, 2016
This is version 97 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.