ID   TCPH_TETPY              Reviewed;         558 AA.
AC   P54409;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=T-complex protein 1 subunit eta;
DE            Short=TCP-1-eta;
DE   AltName: Full=CCT-eta;
OS   Tetrahymena pyriformis.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CGL;
RX   PubMed=8925913; DOI=10.1016/0014-5793(96)00240-2;
RA   Cyrne L., Guerreiro P., Cardoso A.C., Rodrigues-Pousada C., Soares H.;
RT   "The Tetrahymena chaperonin subunit CCT eta gene is coexpressed with CCT
RT   gamma gene during cilia biogenesis and cell sexual reproduction.";
RL   FEBS Lett. 383:277-283(1996).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; U46030; AAC47006.1; -; Genomic_DNA.
DR   PIR; S71337; S71337.
DR   AlphaFoldDB; P54409; -.
DR   SMR; P54409; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd03340; TCP1_eta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012720; Chap_CCT_eta.
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   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; TIGR02345; chap_CCT_eta; 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; Cytoplasm; Nucleotide-binding.
FT   CHAIN           1..558
FT                   /note="T-complex protein 1 subunit eta"
FT                   /id="PRO_0000128369"
FT   REGION          524..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  60896 MW;  7147E15277E635C1 CRC64;
     MMQPTILLLK DGTDTSQGKA QIISNINAVQ SIVEIVKTTL GPRGMDKLIE GNRGATISND
     GATILNLLDI VHPAAKTLVD IAKAQDDEVG DGTTSVCLLA GELLKESKNF IEEGMHPQIV
     TKGYKEALKL ALTFLQENSY SVADKSDGEK REMLLKCAQT SLNSKLLAHY KEFFSEMVVQ
     AVETLDTNLL DKDLIGIKMV TGGSVTDSVL VKGVAFKKTF SYAGFEQQPK KFANPKICLL
     NIELELKAEK ENAEIRIDNP DDYKSIVDAE WELIYEKLRK IVESGAQIVL SKLPIGDLAT
     QYFADRNIFC AGRVDAEDIK RVQKATGSIV QTTVNGLSQD VLGTCGMFEE QQIGAERYNL
     FQDCPHSKSA TIILRGGAEQ FIAEAERSLN DAIMIVRRCM KANKIVPGGG AIELEISRLL
     RLHSRKTEGK VQLVINAFAK ALEVIPKTIA DNAGHDSIQV LNKLRQKHAL ESDQSKNFGV
     DINAVDGIGN NFENFVWEPI IVRKNAFSAA TEAACTILSI DETVRNPKSE QPKAPPGGLR
     RGGPQGMAGL AKNARLGK