ID   TCPG_TETPY              Reviewed;         559 AA.
AC   P54408;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=T-complex protein 1 subunit gamma;
DE            Short=TCP-1-gamma;
DE   AltName: Full=CCT-gamma;
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=7961900; DOI=10.1016/s0021-9258(19)62044-2;
RA   Soares H., Penque D., Mouta C., Rodrigues-Pousada C.;
RT   "A Tetrahymena orthologue of the mouse chaperonin subunit CCT gamma and its
RT   coexpression with tubulin during cilia recovery.";
RL   J. Biol. Chem. 269:29299-29307(1994).
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; Z34885; CAA84368.1; -; Genomic_DNA.
DR   PIR; A55423; A55423.
DR   AlphaFoldDB; P54408; -.
DR   SMR; P54408; -.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IEA:UniProt.
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; cd03337; TCP1_gamma; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012719; Chap_CCT_gamma.
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; TIGR02344; chap_CCT_gamma; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Disulfide bond; Nucleotide-binding.
FT   CHAIN           1..559
FT                   /note="T-complex protein 1 subunit gamma"
FT                   /id="PRO_0000128329"
FT   REGION          537..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        369..375
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   559 AA;  61616 MW;  971E65C3F82A374C CRC64;
     MFQGGHQPIM VLNQNTKRES GKKAQLANIS ASKAVSEIVT STLGPRSMLK MLLDPMGGIV
     MTNDGNAILR EIDVNHPAAK SMIELARVQD EEVGDGTTSV IIMAGEMMSA AKPFIERDIH
     PSIIVTAYYR ALEESIKKIE ELAVPIDVNN DDQVNKALSS CIGTKFTSRW GKLITDLALK
     AVRTIMRGGN LQKLNLEIKR YAKVEKIPGG TLEDSVVLDG VMFNKDITHP KMRRFIKNPR
     VILLDCPLEY KKGESMTNLE MMKETDMTDA LQQEMEELAL MCNDILKHKP DVVITEKGVS
     DLAQHYLLKQ NVSVIRRVRK TDNNRISRVS GATIVNRPEE IQESDVGKKC GLFEVKLIGD
     EYFTFMTECE NPEACSIILR GASKDVLNEM ERNLHDCLAV AKNIFVNPKL VPGGGAIEME
     VSSHLEKISS SIEGLHQLPF RAVAYALEAI PKTLAQNCGV DVVRNITELR AKHNQEGNKF
     IGIEGNSGKI TDMGEANVWE PIAVKLQVYK TAIESACMLL RIDDVVSGLK KQKVAKGGAS
     VTDGNGQEIP ETFGDARDG