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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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Thermosome subunit alphaPRO_0000128398Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
548
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 204Combined sources
Helixi21 – 4020Combined sources
Beta strandi49 – 535Combined sources
Beta strandi59 – 635Combined sources
Helixi65 – 717Combined sources
Helixi77 – 9216Combined sources
Helixi97 – 11620Combined sources
Helixi121 – 14222Combined sources
Helixi151 – 16111Combined sources
Helixi168 – 1703Combined sources
Helixi171 – 18515Combined sources
Beta strandi187 – 1948Combined sources
Helixi197 – 1993Combined sources
Beta strandi200 – 2089Combined sources
Helixi210 – 2123Combined sources
Beta strandi214 – 2229Combined sources
Beta strandi232 – 24211Combined sources
Beta strandi257 – 2593Combined sources
Helixi262 – 28524Combined sources
Beta strandi290 – 2956Combined sources
Helixi299 – 3079Combined sources
Beta strandi311 – 3133Combined sources
Helixi318 – 32811Combined sources
Beta strandi333 – 3353Combined sources
Helixi336 – 3383Combined sources
Helixi341 – 3433Combined sources
Beta strandi345 – 35511Combined sources
Beta strandi358 – 3647Combined sources
Beta strandi370 – 38011Combined sources
Helixi381 – 40323Combined sources
Beta strandi406 – 4094Combined sources
Helixi413 – 42917Combined sources
Helixi431 – 44313Combined sources
Helixi446 – 4549Combined sources
Helixi459 – 47315Combined sources
Beta strandi477 – 4804Combined sources
Turni481 – 4844Combined sources
Beta strandi485 – 4884Combined sources
Turni489 – 4935Combined sources
Beta strandi495 – 4973Combined sources
Helixi498 – 51619Combined sources
Beta strandi520 – 5234Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 9-526.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61112.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

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]
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
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. Positions 9-526.
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

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: December 9, 2015
This is version 60 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.