ID   TCPB_SCHPO              Reviewed;         527 AA.
AC   Q10147;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Probable T-complex protein 1 subunit beta;
DE            Short=TCP-1-beta;
DE   AltName: Full=CCT-beta;
GN   Name=cct2; ORFNames=SPAC1D4.04;
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 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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93213.1; -; Genomic_DNA.
DR   PIR; T38045; T38045.
DR   RefSeq; NP_593017.1; NM_001018416.2.
DR   AlphaFoldDB; Q10147; -.
DR   SMR; Q10147; -.
DR   BioGRID; 278686; 4.
DR   STRING; 4896.SPAC1D4.04.1; -.
DR   MaxQB; Q10147; -.
DR   PaxDb; Q10147; -.
DR   PRIDE; Q10147; -.
DR   EnsemblFungi; SPAC1D4.04.1; SPAC1D4.04.1:pep; SPAC1D4.04.
DR   GeneID; 2542212; -.
DR   KEGG; spo:SPAC1D4.04; -.
DR   PomBase; SPAC1D4.04; cct2.
DR   VEuPathDB; FungiDB:SPAC1D4.04; -.
DR   eggNOG; KOG0363; Eukaryota.
DR   HOGENOM; CLU_008891_6_2_1; -.
DR   InParanoid; Q10147; -.
DR   OMA; YCTGGEI; -.
DR   PhylomeDB; Q10147; -.
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:Q10147; -.
DR   Proteomes; UP000002485; Chromosome I.
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:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
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; cd03336; TCP1_beta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012716; Chap_CCT_beta.
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   PANTHER; PTHR11353:SF23; PTHR11353:SF23; 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; TIGR02341; chap_CCT_beta; 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; Reference proteome.
FT   CHAIN           1..527
FT                   /note="Probable T-complex protein 1 subunit beta"
FT                   /id="PRO_0000128319"
SQ   SEQUENCE   527 AA;  56677 MW;  EFBAF543E38B3B2A CRC64;
     MSLNPHQIFN ESGIQERGEN ARLSSFVGAI AVGDLVKSTL GPKGMDKILQ SNSSGDIVVT
     NDGATILKSI ALDNAAAKVL VNISKVQDDE VGDGTTSVCV FAAELLRQAE IMVNAKIHPQ
     VIIDGYRIAT KTAIDALRAS SIDNSSDPAK FRSDLENIAR TTLSSKILSQ NKNHFAQLAV
     DAVLRLKGST NLDNIQIIKI LGGKLDDSFL DEGFILNKTI GVNCPKVMEN ANILIANTAM
     DTDKVKVFGA RVRVDTTGKL AELERAEREK MKAKVEKIKS HNINCFINRQ LIYNWPEQLF
     ADAGIMSIEH ADFDGIERLS LVTGGEIAST FDHPELVKLG HCKKIEEIII GEDKMIKFSG
     VEAGEACTIV LRGATHQLLD ESERAIHDAL AVLSQTVAES RVTLGGGCAE MLMAKAVEEA
     ATHEPGKKAV AVSAFAKALS QLPTILADNA GFDSSELVAQ LKAAHYDGND TMGLDMDEGE
     IADMRAKGIL EALKLKQAVV SSGSEGAQLL LRVDTILKAA PRPRERM