Q877G8 (Q877G8_METMI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Submitted name: Chaperonin EMBL AAM21720.1
Organism	Methanococcus maripaludis (Methanococcus deltae) EMBL AAM21720.1
Taxonomic identifier	39152 [NCBI]
Taxonomic lineage	cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus

Protein attributes

Sequence length	543 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the TCP-1 chaperonin family. RuleBase RU004187

Ontologies

Keywords
Ligand	ATP-binding RuleBase RU003319 Nucleotide-binding
Molecular function	Chaperone RuleBase RU003319
Technical term	3D-structure PDB 3KFE PDB 3KFB PDB 3IYF PDB 3LOS PDB 3KFK PDB 3IZH PDB 3IZI PDB 3IZJ PDB 3IZK PDB 3IZL PDB 3IZM PDB 3IZN PDB 3J02 PDB 3J03 PDB 3RUQ PDB 3RUS PDB 3RUV PDB 3RUW
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	38 – 40	3	ADP PDB 3KFE
	Nucleotide binding	91 – 94	4	ADP PDB 3KFE
Sites
	Binding site	59	1	ADP PDB 3KFE
	Binding site	160	1	ADP; via carbonyl oxygen PDB 3KFE
	Binding site	404	1	ADP; via amide nitrogen PDB 3KFE
	Binding site	490	1	ADP PDB 3KFE

Sequences

	Sequence		Length	Mass (Da)
	Q877G8 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 3ED9187B0B2EEC89	FASTA	543	58,215
	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

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.
[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 7-519.
[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 7-519.
[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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY099402 Genomic DNA. Translation: AAM21720.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	1-543	[»]
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	7-519	[»]
3IZL	electron microscopy	6.20	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	7-519	[»]
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	7-519	[»]
3J02	electron microscopy	8.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	7-519	[»]
3J03	electron microscopy	4.80	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	7-519	[»]
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	[»]

ProteinModelPortal

Q877G8.

SMR

Q877G8. Positions 7-519.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29771N.

STRING

267377.MMP1515.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

ProtClustDB

CLSK876419.

Family and domain databases

InterPro

IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR012714. Thermosome_arc.
[Graphical view]

PANTHER

PTHR11353. PTHR11353. 1 hit.
PTHR11353:SF27. PTHR11353:SF27. 1 hit.

Pfam

PF00118. Cpn60_TCP1. 1 hit.
[Graphical view]

PRINTS

PR00304. TCOMPLEXTCP1.

SUPFAM

SSF48592. GroEL-ATPase. 1 hit.

TIGRFAMs

TIGR02339. thermosome_arch. 1 hit.

PROSITE

PS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q877G8.

Entry information

Entry name

Q877G8_METMI

Accession

Primary (citable) accession number: Q877G8

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2003
Last sequence update:	June 1, 2003
Last modified:	April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)