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Protein

Thermosome subunit alpha

Gene

thsA

Organism
Thermococcus sp. (strain JCM 11816 / KS-1)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.9. 12506.

Names & Taxonomyi

Protein namesi
Recommended name:
Thermosome subunit alpha
Alternative name(s):
Chaperonin subunit alpha
Thermosome subunit 1
Gene namesi
Name:thsA
OrganismiThermococcus sp. (strain JCM 11816 / KS-1)
Taxonomic identifieri1295125 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001283981 – 548Thermosome subunit alphaAdd BLAST548

Interactioni

Subunit structurei

Forms a Heterooligomeric complex of two stacked eight-membered rings.By similarity

Structurei

Secondary structure

1548
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 20Combined sources4
Helixi21 – 40Combined sources20
Beta strandi49 – 53Combined sources5
Beta strandi59 – 63Combined sources5
Helixi65 – 71Combined sources7
Helixi77 – 92Combined sources16
Helixi97 – 116Combined sources20
Helixi121 – 142Combined sources22
Helixi151 – 161Combined sources11
Helixi168 – 170Combined sources3
Helixi171 – 185Combined sources15
Beta strandi187 – 194Combined sources8
Helixi197 – 199Combined sources3
Beta strandi200 – 208Combined sources9
Helixi210 – 212Combined sources3
Beta strandi214 – 222Combined sources9
Beta strandi232 – 242Combined sources11
Beta strandi257 – 259Combined sources3
Helixi262 – 285Combined sources24
Beta strandi290 – 295Combined sources6
Helixi299 – 307Combined sources9
Beta strandi311 – 313Combined sources3
Helixi318 – 328Combined sources11
Beta strandi333 – 335Combined sources3
Helixi336 – 338Combined sources3
Helixi341 – 343Combined sources3
Beta strandi345 – 355Combined sources11
Beta strandi358 – 364Combined sources7
Beta strandi370 – 380Combined sources11
Helixi381 – 403Combined sources23
Beta strandi406 – 409Combined sources4
Helixi413 – 429Combined sources17
Helixi431 – 443Combined sources13
Helixi446 – 454Combined sources9
Helixi459 – 473Combined sources15
Beta strandi477 – 480Combined sources4
Turni481 – 484Combined sources4
Beta strandi485 – 488Combined sources4
Turni489 – 493Combined sources5
Beta strandi495 – 497Combined sources3
Helixi498 – 516Combined sources19
Beta strandi520 – 523Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q2VX-ray2.40A/B/C/D1-548[»]
1Q3QX-ray2.30A/B/C/D1-548[»]
1Q3RX-ray2.90A/B/C/D1-548[»]
1Q3SX-ray3.00A/B/C/D/E/F/G/H1-548[»]
ProteinModelPortaliP61112.
SMRiP61112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61112.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Family and domain databases

CDDicd03343. cpn60. 1 hit.
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]
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.

P61112-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQLSGQPVV ILPEGTQRYV GRDAQRLNIL AARIIAETVR TTLGPKGMDK
60 70 80 90 100
MLVDSLGDIV VTNDGATILD KIDLQHPAAK MMVEVAKTQD KEAGDGTTTA
110 120 130 140 150
VVIAGELLRK AEELLDQNIH PSIIIKGYAL AAEKAQEILD EIAIRVDPDD
160 170 180 190 200
EETLLKIAAT SITGKNAESH KELLAKLAVE AVKQVAEKKD GKYVVDLDNI
210 220 230 240 250
KFEKKAGEGV EESELVRGVV IDKEVVHPRM PKRVENAKIA LINEALEVKK
260 270 280 290 300
TETDAKINIT SPDQLMSFLE QEEKMLKDMV DHIAQTGANV VFVQKGIDDL
310 320 330 340 350
AQHYLAKYGI MAVRRVKKSD MEKLAKATGA KIVTNVKDLT PEDLGYAEVV
360 370 380 390 400
EERKLAGENM IFVEGCKNPK AVTILIRGGT EHVIDEVERA LEDAVKVVKD
410 420 430 440 450
VMEDGAVLPA GGAPEIELAI RLDEYAKQVG GKEALAIENF ADALKIIPKT
460 470 480 490 500
LAENAGLDTV EMLVKVISEH KNRGLGIGID VFEGKPADML EKGIIEPLRV
510 520 530 540
KKQAIKSASE AAIMILRIDD VIAAKATKPE GGQGGGMPGG MGGMDMGM
Length:548
Mass (Da):59,170
Last modified:May 10, 2004 - v1
Checksum:iD7B4F3889E02A88A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001080 Genomic DNA. Translation: BAA22207.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001080 Genomic DNA. Translation: BAA22207.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q2VX-ray2.40A/B/C/D1-548[»]
1Q3QX-ray2.30A/B/C/D1-548[»]
1Q3RX-ray2.90A/B/C/D1-548[»]
1Q3SX-ray3.00A/B/C/D/E/F/G/H1-548[»]
ProteinModelPortaliP61112.
SMRiP61112.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.6.4.9. 12506.

Miscellaneous databases

EvolutionaryTraceiP61112.

Family and domain databases

CDDicd03343. cpn60. 1 hit.
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]
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...

Entry informationi

Entry nameiTHSA_THEK1
AccessioniPrimary (citable) accession number: P61112
Secondary accession number(s): O24729, Q9Y8I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: November 2, 2016
This is version 62 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

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.