ID   TCPZ_SCHPO              Reviewed;         535 AA.
AC   O94515;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=T-complex protein 1 subunit zeta;
DE            Short=TCP-1-zeta;
DE   AltName: Full=CCT-zeta;
GN   Name=cct6; ORFNames=SPBC646.11;
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329671; CAA22815.1; -; Genomic_DNA.
DR   PIR; T40587; T40587.
DR   RefSeq; NP_595369.1; NM_001021277.2.
DR   AlphaFoldDB; O94515; -.
DR   SMR; O94515; -.
DR   BioGRID; 277643; 4.
DR   IntAct; O94515; 1.
DR   STRING; 4896.SPBC646.11.1; -.
DR   iPTMnet; O94515; -.
DR   MaxQB; O94515; -.
DR   PaxDb; O94515; -.
DR   PRIDE; O94515; -.
DR   EnsemblFungi; SPBC646.11.1; SPBC646.11.1:pep; SPBC646.11.
DR   GeneID; 2541128; -.
DR   KEGG; spo:SPBC646.11; -.
DR   PomBase; SPBC646.11; cct6.
DR   VEuPathDB; FungiDB:SPBC646.11; -.
DR   eggNOG; KOG0359; Eukaryota.
DR   HOGENOM; CLU_008891_3_1_1; -.
DR   InParanoid; O94515; -.
DR   OMA; LHPRIMT; -.
DR   PhylomeDB; O94515; -.
DR   Reactome; R-SPO-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-SPO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:O94515; -.
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:0005634; C:nucleus; 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; cd03342; TCP1_zeta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012722; Chap_CCT_zeta.
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; TIGR02347; chap_CCT_zeta; 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..535
FT                   /note="T-complex protein 1 subunit zeta"
FT                   /id="PRO_0000128361"
SQ   SEQUENCE   535 AA;  58548 MW;  9FABB5CA3CAF511E CRC64;
     MLSLLNPKAE SIQRAQALQV NISAAIGLQD VLKSNLGPTG TTKMLVDGAG AIKLTKDGKV
     LLTEMQIQNP TASCIAKAAT AQDDATGDGT TSVCLLVGEL LKQAELYIRE GLHPSLISDG
     FNLAKNEALT FLDSFKTDFE VDREVLLNVA KTSLSTKISS KVVESLAPAV VDAILTIRRP
     DEPIDLHMVE IMKMQNRSAS DTQLIRGLLL DHGARHPDMP KQVKNAYILI LNVSLEYEKS
     EINSGFFYST SEQRERLVES ERKFVDNKLR KIVELKKEVC ERDPTANFVI INQKGIDPLS
     LDVLAKNGIM ALRRAKRRNM ERLQLACGGV AQNSVDDLNP EVLGWAGSVY ERTLGEEKYT
     FVEDVKDPKS ATILIHGPNT YTIQQIQDAT RDGLRAVKNA VEDNCLIVGA GAFEVACAAH
     LRNKFAAKEV KGKAKMGVYA YADALLIIPK TLAANSSYDT QDAIVALQEE ASEGYKVGLD
     LKTGMPFDPE VEGIYDNYRV IRHMLHSATV IASNLISVDQ ILRAGRSSLK EGPPQ