ID   TCPQ_SCHPO              Reviewed;         546 AA.
AC   P78921; O74816;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 3.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Probable T-complex protein 1 subunit theta;
DE            Short=TCP-1-theta;
DE   AltName: Full=CCT-theta;
GN   Name=cct8; ORFNames=SPBC337.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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 (By 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13933.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D89272; BAA13933.1; ALT_INIT; mRNA.
DR   EMBL; CU329671; CAA21275.1; -; Genomic_DNA.
DR   PIR; T40258; T40258.
DR   PIR; T43202; T43202.
DR   RefSeq; NP_595406.1; NM_001021313.2.
DR   AlphaFoldDB; P78921; -.
DR   SMR; P78921; -.
DR   BioGRID; 276835; 6.
DR   IntAct; P78921; 1.
DR   STRING; 4896.SPBC337.05c.1; -.
DR   iPTMnet; P78921; -.
DR   MaxQB; P78921; -.
DR   PaxDb; P78921; -.
DR   PRIDE; P78921; -.
DR   EnsemblFungi; SPBC337.05c.1; SPBC337.05c.1:pep; SPBC337.05c.
DR   GeneID; 2540305; -.
DR   KEGG; spo:SPBC337.05c; -.
DR   PomBase; SPBC337.05c; cct8.
DR   VEuPathDB; FungiDB:SPBC337.05c; -.
DR   eggNOG; KOG0362; Eukaryota.
DR   HOGENOM; CLU_008891_4_2_1; -.
DR   InParanoid; P78921; -.
DR   OMA; WGLKYAV; -.
DR   PhylomeDB; P78921; -.
DR   Reactome; R-SPO-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P78921; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IDA:PomBase.
DR   GO; GO:0005856; C:cytoskeleton; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
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; ISO:PomBase.
DR   GO; GO:0006457; P:protein folding; ISO:PomBase.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..546
FT                   /note="Probable T-complex protein 1 subunit theta"
FT                   /id="PRO_0000128377"
FT   REGION          527..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        104
FT                   /note="V -> I (in Ref. 1; BAA13933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107..112
FT                   /note="TGELLA -> SGALLL (in Ref. 1; BAA13933)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   546 AA;  59956 MW;  61EEBF8CE3A4ACEE CRC64;
     MALRVPKASG PQLFREGYRI MQGVEDAVIR NCNAIRELSE ITRTSLGPNG KNKIVVNHLQ
     QTFLTNDAAT IIRELEVIHP AAKLVVDATQ QQENELGDAA NFVVVFTGEL LAKAENMIRM
     GLTPLEIAKG YEMALSHTME VLEEICADKI ETVESEKELI KAIRTCISSK QYGNEDFLSD
     LVAKAILTVL PKDPSKFNVD NIRVVKIMGS SLYNSQVVKG MVFPREPEGT VTRSKEAKVA
     VFSCPLDISQ TETKGTVLLH NAQEMLDFSK GEENLIESHI KEIYDAGVRV VVTSGNVNDL
     VLHYLNRFEI LVIRVPSKFE LRRLCRVVGA TPLARMGVPM PEEMGSVDVV ETIEIGGDRV
     TVFRQVEDIT RTATIVLRGA TKTYLDDLER AIDDGVNIVK ALVKDNRLIF GAGASDMQLC
     IRLISVGEKT PGIYQHAIKQ YGEAFEVVPR TISENAGLDP TDVISKLYAA HHKENGESIG
     VDVECENDGT LDAKEAGIFD VLLAKKSAIR LATETVLTVL NVDQVVMSKP AGGPKPPGPN
     PHWDDD