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Q877G8 (Q877G8_METMI) Unreviewed, UniProtKB/TrEMBL

Last modified January 22, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the TCP-1 chaperonin family. RuleBase RU004187

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding38 – 414ADP PDB 3KFE PDB 3RUQ PDB 3RUS PDB 3RUW
Nucleotide binding91 – 955ADP PDB 3KFE PDB 3RUQ PDB 3RUS PDB 3RUW
Nucleotide binding160 – 1612ADP PDB 3KFE PDB 3RUQ PDB 3RUW
Region91 – 944Sulfate 1 binding PDB 3KFE
Region307 – 3082Sulfate 3 binding PDB 3RUS PDB 3RUW

Sites

Binding site591ADP PDB 3KFE
Binding site601Sulfate 1 PDB 3KFE
Binding site661Sulfate 2
Binding site831Sulfate 2
Binding site1611Sulfate 1 PDB 3KFE
Binding site2161Sulfate 3 PDB 3RUS PDB 3RUW
Binding site2181Sulfate 5 PDB 3RUS PDB 3RUW
Binding site2251Sulfate 4 (covalent) PDB 3RUW
Binding site2251Sulfate 5 PDB 3RUS PDB 3RUW
Binding site4041ADP; via amide nitrogen PDB 3KFE PDB 3RUQ PDB 3RUS PDB 3RUW
Binding site4901ADP PDB 3KFE PDB 3RUQ PDB 3RUS PDB 3RUW

Sequences

Sequence LengthMass (Da)Tools
Q877G8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3ED9187B0B2EEC89

FASTA54358,215
        10         20         30         40         50         60 
MSQQPGVLPE NMKRYMGRDA QRMNILAGRI IAETVRSTLG PKGMDKMLVD DLGDVVVTND 

        70         80         90        100        110        120 
GVTILREMSV EHPAAKMLIE VAKTQEKEVG DGTTTAVVVA GELLRKAEEL LDQNVHPTIV 

       130        140        150        160        170        180 
VKGYQAAAQK AQELLKTIAC EVGAQDKEIL TKIAMTSITG KGAEKAKEKL AEIIVEAVSA 

       190        200        210        220        230        240 
VVDDEGKVDK DLIKIEKKSG ASIDDTELIK GVLVDKERVS AQMPKKVTDA KIALLNCAIE 

       250        260        270        280        290        300 
IKETETDAEI RITDPAKLME FIEQEEKMLK DMVAEIKASG ANVLFCQKGI DDLAQHYLAK 

       310        320        330        340        350        360 
EGIVAARRVK KSDMEKLAKA TGANVITNIK DLSAQDLGDA GLVEERKISG DSMIFVEECK 

       370        380        390        400        410        420 
HPKAVTMLIR GTTEHVIEEV ARAVDDAVGV VGCTIEDGRI VSGGGSTEVE LSMKLREYAE 

       430        440        450        460        470        480 
GISGREQLAV RAFADALEVI PRTLAENAGL DAIEILVKVR AAHASNGNKC AGLNVFTGAV 

       490        500        510        520        530        540 
EDMCENGVVE PLRVKTQAIQ SAAESTEMLL RIDDVIAAEK LRGAPDMGDM GGMPGMGGMP 


GMM 

« Hide

References

[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: LL EMBL AAM21720.1.
[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 SULFATE.
[3]"Mechanism of folding chamber closure in a group II chaperonin."
Zhang J., Baker M.L., Schroder G.F., Douglas N.R., Reissmann S., Jakana J., Dougherty M., Fu C.J., Levitt M., Ludtke S.J., Frydman J., Chiu W.
Nature 463:379-383(2010) [PubMed] [Europe PMC] [Abstract]
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]"Mechanism of nucleotide sensing in group II chaperonins."
Pereira J.H., Ralston C.Y., Douglas N.R., Kumar R., Lopez T., McAndrew R.P., Knee K.M., King J.A., Frydman J., Adams P.D.
EMBO J. 31:731-740(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) IN COMPLEX WITH ADP AND SULFATE.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY099402 Genomic DNA. Translation: AAM21720.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ877G8.
SMRQ877G8. Positions 7-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29771N.
MINTMINT-8373072.
STRING267377.MMP1515.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

ProtClustDBCLSK876419.

Family and domain databases

Gene3D1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProIPR017998. 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]
PANTHERPTHR11353. PTHR11353. 1 hit.
PTHR11353:SF27. PTHR11353:SF27. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSPR00304. TCOMPLEXTCP1.
SUPFAMSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsTIGR02339. thermosome_arch. 1 hit.
PROSITEPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ877G8.

Entry information

Entry nameQ877G8_METMI
AccessionPrimary (citable) accession number: Q877G8
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: January 22, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)