ID   THSA_THEK8              Reviewed;         549 AA.
AC   O24731;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Thermosome subunit alpha;
DE   AltName: Full=Chaperonin subunit alpha;
DE   AltName: Full=Thermosome subunit 1;
GN   Name=thsA;
OS   Thermococcus sp. (strain KS-8).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus; unclassified Thermococcus.
OX   NCBI_TaxID=79680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Yoshida T., Yohda M., Ohta T., Iida T., Maruyama T., Kagawa Y.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC       and has a weak ATPase activity. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked eight-membered
CC       rings. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AB001082; BAA22209.1; -; Genomic_DNA.
DR   AlphaFoldDB; O24731; -.
DR   SMR; O24731; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd03343; cpn60; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   InterPro; IPR012714; Thermosome_arc.
DR   PANTHER; PTHR11353; PTHR11353; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02339; thermosome_arch; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..549
FT                   /note="Thermosome subunit alpha"
FT                   /id="PRO_0000128413"
FT   REGION          529..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  59410 MW;  D9FB40443F736DA8 CRC64;
     MAQLSGQPVV ILPEGTQRYV GRDAQRLNIL AARIIAETVR TTLGPKGMDK MLVDSLGDIV
     VTNDGATILD KIDLQHPAAK MMVEVAKTQD KEAGDGTTTA VVIAGELLRK AEELLDQNIH
     PSIIIKGYAL AAEKAQEILE EIAIKVNPDD EETLLRIAMT SITGKNAESH KELLAKLAVD
     AVKQVAEKKD GKYVVDLDNI KFEKKAGEGV EESELVRGVV IDKEVVHPRM PKRVEGAKIA
     LINEALEVKK TETDAKINIT SPDQLMSFLE QEEKMLKDMV DHIAQTGANV VFVQKGIDDL
     AQHYLAKYGI MAVRRVKKSD MEKLAKATGA KIVTNVKDLT PEDLGYAEIV EERKLAGENM
     IFVEGCKNPK AVTILIRGGT EHVIDEVERA LEDAVKVVKD VMEDGAVLPA GGAPEIELAI
     SVDEYAKQVG GKEALAIENF ADALKIIPKT LAENAGLDTV EILVKVISEH KNKGLGIGID
     VFAGEPADML ERGIIAPLRV TKQAIKSARA AIMILRIDDV IAAKVSKPEG RQGAECPPNG
     CMGGMDMRM