ID   TCPQ_CANAX              Reviewed;         540 AA.
AC   P47828;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=T-complex protein 1 subunit theta;
DE            Short=TCP-1-theta;
DE   AltName: Full=CCT-theta;
GN   Name=CCT8;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX   PubMed=8771707;
RX   DOI=10.1002/(sici)1097-0061(199605)12:6<523::aid-yea962>3.0.co;2-c;
RA   Stoldt V., Rademacher F., Kehren V., Ernst J.F., Sherman F.;
RT   "Review: the Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae
RT   and other yeasts.";
RL   Yeast 12:523-529(1996).
RN   [2]
RP   SEQUENCE REVISION.
RA   Ernst J.F.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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. In yeast may play a role in mitotic spindle formation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; U37371; AAC31764.1; -; Genomic_DNA.
DR   AlphaFoldDB; P47828; -.
DR   SMR; P47828; -.
DR   VEuPathDB; FungiDB:C1_00110W_A; -.
DR   VEuPathDB; FungiDB:CAWG_01354; -.
DR   BRENDA; 3.6.4.B10; 1096.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IEA:EnsemblFungi.
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:EnsemblFungi.
DR   GO; GO:0051086; P:chaperone mediated protein folding independent of cofactor; IEA:EnsemblFungi.
DR   CDD; cd03341; TCP1_theta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012721; Chap_CCT_theta.
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; 2.
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; TIGR02346; chap_CCT_theta; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding.
FT   CHAIN           1..540
FT                   /note="T-complex protein 1 subunit theta"
FT                   /id="PRO_0000128376"
SQ   SEQUENCE   540 AA;  58918 MW;  F962285DA6EB03DE CRC64;
     MSLKLPQAPN SGLFKQGYSS FSNADGAIIR NVEAVREIAS ILLTSMGPSG RNKIIVNKLG
     KKFITNDAAT MLNELEIVHP VVKILIQASK QQEFEMGDNT NLVIILAGEF LNVAEKLLTL
     GLNVSEIIQG FNLANKFVMK TLDELVVEKV ESFETDLLKA VKPVIAAKQY GVEDTIAKLV
     VDAVALVMKN GSFNVDNIRV VKVMGASLSQ SQVVKGMVFP REPEGTVKNA DQIQSCRVYQ
     PHRYFHHRNQ RYSCSSTMPR KCLISPRAKN NSWTSCARKS TIQGLRWLLP GSSVGELALH
     YLNKYGILVL RVPSKFDLRR ICQVCGATPL PRLGAPTPDE MGEIDIIETK EIGGDRVTIF
     RQDESSSRTA TIVVRGATQN NLDDIERAID DGVNSIKGLI KDNRLLPGAG AVEIELMKRI
     TAYQSTPGLL QLAIKSFAKA FEVIPRVLAE TSGHDSSEIL SKLHAAHAED TGLRAGIDID
     SGEVADTAVL DILATKKSAI DLAVDATNTI LSIDQIIMAK RAGGPVMPQQ PRPGNWDQDD