ID   TCPH_TETTH              Reviewed;         353 AA.
AC   P54410;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=T-complex protein 1 subunit eta;
DE            Short=TCP-1-eta;
DE   AltName: Full=CCT-eta;
DE   Flags: Fragment;
OS   Tetrahymena thermophila.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SB1917;
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; U46028; AAC47007.1; -; Genomic_DNA.
DR   PIR; S71338; S71338.
DR   AlphaFoldDB; P54410; -.
DR   SMR; P54410; -.
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   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   PANTHER; PTHR11353:SF22; PTHR11353:SF22; 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   PROSITE; PS00995; TCP1_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding.
FT   CHAIN           <1..>353
FT                   /note="T-complex protein 1 subunit eta"
FT                   /id="PRO_0000128370"
FT   NON_TER         1
FT   NON_TER         353
SQ   SEQUENCE   353 AA;  39050 MW;  BE37AE2AA95FA1EC CRC64;
     NDGATILNLL DIVHPAAKTL VDIAKAQDDE VGDGTTSVCL LAGELLKESK YFIEEGMHPQ
     IITKGYKEAL KLALQFLHEN AHSVADKNET EKREMLIKCA QTSLNSKLLA HYKEFFSELV
     VQAVETLETN LLDKDLIGIK MVTGGSVTDS FLVSGVAFKK TFSYAGFEQQ PKKFNNPKIC
     LLNIELELKA EKENAEIRIE NPDDYKSIVD AEWELIYEKL RKIVESGANI VLSKLPIGDL
     ATQYFADRNI FCAGRVDAED MKRVQKSTGA IVQTTVNGLT EDVLGTCNQF EEVQIGAERY
     NLFKDCPHSK SATIILRGGA EQFIAEAERS LNDAIMIVRR CMKANKIVPG GGA