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Q877G8

- Q877G8_METMI

UniProt

Q877G8 - Q877G8_METMI

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Protein
Submitted name: Chaperonin
Gene
N/A
Organism
Methanococcus maripaludis (Methanococcus deltae)
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei59 – 591ADP
Binding sitei66 – 661Sulfate 2
Binding sitei83 – 831Sulfate 2
Binding sitei404 – 4041ADP; via amide nitrogenImported
Binding sitei490 – 4901ADPImported

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 414ADPImported
Nucleotide bindingi91 – 955ADPImported
Nucleotide bindingi160 – 1612ADP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
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

Interactioni

Protein-protein interaction databases

DIPiDIP-29771N.
MINTiMINT-8373072.
STRINGi267377.MMP1515.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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/P268-519[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
3IZLelectron microscopy6.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P268-519[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
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/P268-519[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
3J02electron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P269-519[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
3J03electron microscopy4.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P269-519[»]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P7-240[»]
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.

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.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. 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

MSQQPGVLPE NMKRYMGRDA QRMNILAGRI IAETVRSTLG PKGMDKMLVD    50
DLGDVVVTND GVTILREMSV EHPAAKMLIE VAKTQEKEVG DGTTTAVVVA 100
GELLRKAEEL LDQNVHPTIV VKGYQAAAQK AQELLKTIAC EVGAQDKEIL 150
TKIAMTSITG KGAEKAKEKL AEIIVEAVSA VVDDEGKVDK DLIKIEKKSG 200
ASIDDTELIK GVLVDKERVS AQMPKKVTDA KIALLNCAIE IKETETDAEI 250
RITDPAKLME FIEQEEKMLK DMVAEIKASG ANVLFCQKGI DDLAQHYLAK 300
EGIVAARRVK KSDMEKLAKA TGANVITNIK DLSAQDLGDA GLVEERKISG 350
DSMIFVEECK HPKAVTMLIR GTTEHVIEEV ARAVDDAVGV VGCTIEDGRI 400
VSGGGSTEVE LSMKLREYAE GISGREQLAV RAFADALEVI PRTLAENAGL 450
DAIEILVKVR AAHASNGNKC AGLNVFTGAV EDMCENGVVE PLRVKTQAIQ 500
SAAESTEMLL RIDDVIAAEK LRGAPDMGDM GGMPGMGGMP GMM 543
Length:543
Mass (Da):58,215
Last modified:June 1, 2003 - v1
Checksum:i3ED9187B0B2EEC89
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY099402 Genomic DNA. Translation: AAM21720.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY099402 Genomic DNA. Translation: AAM21720.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IYF electron microscopy 8.00 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-240 [» ]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 268-543 [» ]
3IZH electron microscopy 11.00 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 7-519 [» ]
3IZI electron microscopy 6.70 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 7-519 [» ]
3IZJ electron microscopy 6.90 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 7-519 [» ]
3IZK electron microscopy 4.90 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 268-519 [» ]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 7-240 [» ]
3IZL electron microscopy 6.20 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 268-519 [» ]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 7-240 [» ]
3IZM electron microscopy 7.20 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 7-519 [» ]
3IZN electron microscopy 6.40 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 268-519 [» ]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 7-240 [» ]
3J02 electron microscopy 8.00 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 269-519 [» ]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 7-240 [» ]
3J03 electron microscopy 4.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 269-519 [» ]
A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 7-240 [» ]
3J3X electron microscopy 4.30 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-532 [» ]
3KFB X-ray 3.20 A/B/C/D/E/F/G/H 1-543 [» ]
3KFE X-ray 3.50 A/B/C/D/E/F/G/H 1-543 [» ]
3KFK X-ray 6.00 A/B/C/D 1-543 [» ]
3LOS electron microscopy 4.30 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-543 [» ]
3RUQ X-ray 2.80 A/B/C/D 1-543 [» ]
3RUS X-ray 2.34 A/B/C/D 1-543 [» ]
3RUV X-ray 2.24 A/B/C/D 1-543 [» ]
3RUW X-ray 2.70 A/B/C/D 1-543 [» ]
ProteinModelPortali Q877G8.
SMRi Q877G8. Positions 7-519.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29771N.
MINTi MINT-8373072.
STRINGi 267377.MMP1515.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q877G8.

Family and domain databases

Gene3Di 1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProi IPR017998. 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 ]
PANTHERi PTHR11353. PTHR11353. 1 hit.
Pfami PF00118. Cpn60_TCP1. 1 hit.
[Graphical view ]
PRINTSi PR00304. TCOMPLEXTCP1.
SUPFAMi SSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsi TIGR02339. thermosome_arch. 1 hit.
PROSITEi PS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
  3. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS).
  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 268-519 AND 7-240.
  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 269-519 AND 7-240.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) IN COMPLEX WITH ADP.
  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: September 3, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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