ID   TCPA_TETPY              Reviewed;         547 AA.
AC   O15891;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=T-complex protein 1 subunit alpha;
DE            Short=TCP-1-alpha;
DE   AltName: Full=CCT-alpha;
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=9337846; DOI=10.1042/bj3260021;
RA   Soares H., Cyrne L., Casalou C., Ehmann B., Rodrigues-Pousada C.;
RT   "The third member of the Tetrahymena CCT subunit gene family, TpCCT alpha,
RT   encodes a component of the hetero-oligomeric chaperonin complex.";
RL   Biochem. J. 326:21-29(1997).
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; U85397; AAC47799.1; -; Genomic_DNA.
DR   AlphaFoldDB; O15891; -.
DR   SMR; O15891; -.
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; cd03335; TCP1_alpha; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012715; Chap_CCT_alpha.
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; TIGR02340; chap_CCT_alpha; 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..547
FT                   /note="T-complex protein 1 subunit alpha"
FT                   /id="PRO_0000128312"
SQ   SEQUENCE   547 AA;  59543 MW;  44481A31B3C3EC1E CRC64;
     MAPSVGILGE RDQGQDVRTN NVTAVMAIAN IVKSSLGPQG LDKMLVDDVG DVTITNDGAT
     ILRQLEVQHP AAKVIVELSQ LQDKEVGDGT TSVVILAAEL LKRANELIKN KVHPTSIITG
     FKIAAKEACT YIKEHLAISV EELGREALIN AAKTSMSSKL IGPESNLFSQ IVVDAVESVK
     MTNLMGDTKY PIKNVKIIKS HGQSTLQSQL IRGYVLQTQR CDQQMKTRIE KAKIALLDFN
     LNKFRLQMGI QILVNDPKNL EKIRFKECEI LKERCKKIIE AGANVIITSA GMDDVATKYL
     VEAGVMGLRR VDKHDLRRLA KATGGTIVTT LATPEGDEVF EASYLGECAE VYEEAVGDND
     CIFFKGTKRA NCASIIIRGA NEFMVDEVDR SLHDSLCVVK RTLESGYVVP GGGAVEIALS
     IKLEDFARTL GTKEQTAVAE FCEALNIIPK VLAANAAQDA TELVSKLRAL HAASQSSDDP
     AKKELKNCGL DLSLGKVRNN VKAGVLEPMV SKIKSLRFAT EAAITILRID DMIKLNPQNE
     ELPQGRH