ID   TCPQ_CAEBR              Reviewed;         548 AA.
AC   A8X6I9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=T-complex protein 1 subunit theta {ECO:0000250|UniProtKB:Q9N358};
DE            Short=TCP-1-theta {ECO:0000250|UniProtKB:Q9N358};
DE   AltName: Full=CCT-theta {ECO:0000250|UniProtKB:Q9N358};
GN   Name=cct-8 {ECO:0000312|EMBL:CAP28250.1}; ORFNames=CBG08425;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP28250.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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. Required for correct subcellular localization of pgl-1 (By
CC       similarity). {ECO:0000250|UniProtKB:P50990,
CC       ECO:0000250|UniProtKB:Q9N358}.
CC   -!- SUBUNIT: Heterooligomeric complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50990}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000255}.
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DR   EMBL; HE601100; CAP28250.1; -; Genomic_DNA.
DR   RefSeq; XP_002634608.1; XM_002634562.1.
DR   AlphaFoldDB; A8X6I9; -.
DR   SMR; A8X6I9; -.
DR   STRING; 6238.CBG08425; -.
DR   EnsemblMetazoa; CBG08425.1; CBG08425.1; WBGene00030217.
DR   GeneID; 8576601; -.
DR   KEGG; cbr:CBG_08425; -.
DR   CTD; 8576601; -.
DR   WormBase; CBG08425; CBP02058; WBGene00030217; Cbr-cct-8.
DR   eggNOG; KOG0362; Eukaryota.
DR   HOGENOM; CLU_008891_4_2_1; -.
DR   InParanoid; A8X6I9; -.
DR   OMA; WGLKYAV; -.
DR   OrthoDB; 617040at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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; 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; 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; Reference proteome.
FT   CHAIN           1..548
FT                   /note="T-complex protein 1 subunit theta"
FT                   /id="PRO_0000394402"
FT   REGION          528..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  59608 MW;  0E233EFBDB7719C3 CRC64;
     MAMKIPKSGY NRFMKEGAQH FKGTDEAVQR NIEACTELAS QIRSAYGPNG MNKMVINHIE
     KLFVTNDAAT ILKELEIQHP AAKIIIMATE MQEKQIGDNT NTVVILAAAL LEHASNLINM
     GMTPQEVAAG YEQAAEKALE ILPSLVVKEA SDMKNIEEVR QYLRSAITSK QYDNEDVIAD
     LVAKACVTTC PANSYNFNVD NIRICKIIGS GVHTSKVMNG MVFKRGAEGE IRSAQDARIA
     VYTCPFDLTQ TETKGTVLIE NADELVNFSK GEESEVEEQV KAIADNGVKV VVAAGKFGDL
     YLHFLNKYKI MAVRLTSKFD LRRLCRTVGA QPQARICAPA VNLLGHCDSV SVTEIGDENV
     VVFDKNSETG KVATIIIRGS SQSRIDDVER AVDDAVNTYK ALTKDGKLLA GAGAVEIELA
     KEIESYGAKA PGLEQYAIKK FAHALETLPK AIAENAGMPT TETLTKLYAE HVNGKKNAGI
     DVWKREVMDA VAHNIFDLYA GKRLAIKLAT DAAATILKVD QIIMAKQATG GPKPRGPKQQ
     DEDDDGMA