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Protein
Submitted name:

Chaperonin

Gene
N/A
Organism
Methanococcus maripaludis (Methanococcus deltae)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei59 – 591ADP
Binding sitei386 – 3861ATP analogCombined sources
Binding sitei404 – 4041ADP; via amide nitrogen
Binding sitei404 – 4041ATP analog; via amide nitrogenCombined sources
Binding sitei474 – 4741ATP analogCombined sources
Binding sitei490 – 4901ADP
Binding sitei490 – 4901ATP analogCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 414ADP
Nucleotide bindingi38 – 403ATP analogCombined sources
Nucleotide bindingi59 – 613ATP analogCombined sources
Nucleotide bindingi91 – 955ADP
Nucleotide bindingi91 – 955ATP analogCombined sources
Nucleotide bindingi160 – 1612ADP
Nucleotide bindingi160 – 1612ATP analogCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

ChaperoneUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
ChaperoninImported
OrganismiMethanococcus maripaludis (Methanococcus deltae)Imported
Taxonomic identifieri39152 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi237 ↔ 286Combined sources
Disulfide bondi470 ↔ 484

Interactioni

Protein-protein interaction databases

DIPiDIP-29771N.
MINTiMINT-8373072.
STRINGi444158.MmarC6_1157.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYFelectron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P268-543[»]
3IZHelectron microscopy11.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-519[»]
3IZIelectron microscopy6.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-519[»]
3IZJelectron microscopy6.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-519[»]
3IZKelectron microscopy4.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P268-519[»]
3IZLelectron microscopy6.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P268-519[»]
3IZMelectron microscopy7.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-519[»]
3IZNelectron microscopy6.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P268-519[»]
3J02electron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P269-519[»]
3J03electron microscopy4.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P269-519[»]
3J3Xelectron microscopy4.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-532[»]
3KFBX-ray3.20A/B/C/D/E/F/G/H1-543[»]
3KFEX-ray3.50A/B/C/D/E/F/G/H1-543[»]
3KFKX-ray6.00A/B/C/D1-543[»]
3LOSelectron microscopy4.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-543[»]
3RUQX-ray2.80A/B/C/D1-543[»]
3RUSX-ray2.34A/B/C/D1-543[»]
3RUVX-ray2.24A/B/C/D1-543[»]
3RUWX-ray2.70A/B/C/D1-543[»]
ProteinModelPortaliQ877G8.
SMRiQ877G8. Positions 7-519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ877G8.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.UniRule annotation

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
IPR012714. Thermosome_arc.
[Graphical view]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02339. thermosome_arch. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q877G8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQQPGVLPE NMKRYMGRDA QRMNILAGRI IAETVRSTLG PKGMDKMLVD
60 70 80 90 100
DLGDVVVTND GVTILREMSV EHPAAKMLIE VAKTQEKEVG DGTTTAVVVA
110 120 130 140 150
GELLRKAEEL LDQNVHPTIV VKGYQAAAQK AQELLKTIAC EVGAQDKEIL
160 170 180 190 200
TKIAMTSITG KGAEKAKEKL AEIIVEAVSA VVDDEGKVDK DLIKIEKKSG
210 220 230 240 250
ASIDDTELIK GVLVDKERVS AQMPKKVTDA KIALLNCAIE IKETETDAEI
260 270 280 290 300
RITDPAKLME FIEQEEKMLK DMVAEIKASG ANVLFCQKGI DDLAQHYLAK
310 320 330 340 350
EGIVAARRVK KSDMEKLAKA TGANVITNIK DLSAQDLGDA GLVEERKISG
360 370 380 390 400
DSMIFVEECK HPKAVTMLIR GTTEHVIEEV ARAVDDAVGV VGCTIEDGRI
410 420 430 440 450
VSGGGSTEVE LSMKLREYAE GISGREQLAV RAFADALEVI PRTLAENAGL
460 470 480 490 500
DAIEILVKVR AAHASNGNKC AGLNVFTGAV EDMCENGVVE PLRVKTQAIQ
510 520 530 540
SAAESTEMLL RIDDVIAAEK LRGAPDMGDM GGMPGMGGMP GMM
Length:543
Mass (Da):58,215
Last modified:June 1, 2003 - v1
Checksum:i3ED9187B0B2EEC89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY099402 Genomic DNA. Translation: AAM21720.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY099402 Genomic DNA. Translation: AAM21720.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYFelectron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P268-543[»]
3IZHelectron microscopy11.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-519[»]
3IZIelectron microscopy6.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-519[»]
3IZJelectron microscopy6.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-519[»]
3IZKelectron microscopy4.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P268-519[»]
3IZLelectron microscopy6.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P268-519[»]
3IZMelectron microscopy7.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-519[»]
3IZNelectron microscopy6.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P268-519[»]
3J02electron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P269-519[»]
3J03electron microscopy4.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P269-519[»]
3J3Xelectron microscopy4.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-532[»]
3KFBX-ray3.20A/B/C/D/E/F/G/H1-543[»]
3KFEX-ray3.50A/B/C/D/E/F/G/H1-543[»]
3KFKX-ray6.00A/B/C/D1-543[»]
3LOSelectron microscopy4.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-543[»]
3RUQX-ray2.80A/B/C/D1-543[»]
3RUSX-ray2.34A/B/C/D1-543[»]
3RUVX-ray2.24A/B/C/D1-543[»]
3RUWX-ray2.70A/B/C/D1-543[»]
ProteinModelPortaliQ877G8.
SMRiQ877G8. Positions 7-519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29771N.
MINTiMINT-8373072.
STRINGi444158.MmarC6_1157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ877G8.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
IPR012714. Thermosome_arc.
[Graphical view]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02339. thermosome_arch. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis."
    Kusmierczyk A.R., Martin J.
    Biochem. J. 371:669-673(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: LLImported.
  2. "Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle."
    Pereira J.H., Ralston C.Y., Douglas N.R., Meyer D., Knee K.M., Goulet D.R., King J.A., Frydman J., Adams P.D.
    J. Biol. Chem. 285:27958-27966(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH ADP AND ATP ANALOG, DISULFIDE BONDS.
  3. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS), DISULFIDE BONDS.
  4. "Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber."
    Douglas N.R., Reissmann S., Zhang J., Chen B., Jakana J., Kumar R., Chiu W., Frydman J.
    Cell 144:240-252(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 7-240 AND 268-519.
  5. "Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure."
    Zhang J., Ma B., DiMaio F., Douglas N.R., Joachimiak L.A., Baker D., Frydman J., Levitt M., Chiu W.
    Structure 19:633-639(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS) OF 7-240 AND 269-519.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) IN COMPLEX WITH ADP AND ATP ANALOG.
  7. "Cryo-EM model validation using independent map reconstructions."
    DiMaio F., Zhang J., Chiu W., Baker D.
    Protein Sci. 22:865-868(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) OF 1-532.

Entry informationi

Entry nameiQ877G8_METMI
AccessioniPrimary (citable) accession number: Q877G8
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.