ID   TCPA_SCHPO              Reviewed;         556 AA.
AC   O94501;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=T-complex protein 1 subunit alpha;
DE            Short=TCP-1-alpha;
DE   AltName: Full=CCT-alpha;
GN   Name=cct1; ORFNames=SPBC12D12.03;
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}.
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DR   EMBL; CU329671; CAA22677.1; -; Genomic_DNA.
DR   PIR; T39383; T39383.
DR   RefSeq; NP_595949.1; NM_001021858.2.
DR   AlphaFoldDB; O94501; -.
DR   SMR; O94501; -.
DR   BioGRID; 276245; 5.
DR   IntAct; O94501; 1.
DR   STRING; 4896.SPBC12D12.03.1; -.
DR   iPTMnet; O94501; -.
DR   MaxQB; O94501; -.
DR   PaxDb; O94501; -.
DR   PRIDE; O94501; -.
DR   EnsemblFungi; SPBC12D12.03.1; SPBC12D12.03.1:pep; SPBC12D12.03.
DR   GeneID; 2539691; -.
DR   KEGG; spo:SPBC12D12.03; -.
DR   PomBase; SPBC12D12.03; cct1.
DR   VEuPathDB; FungiDB:SPBC12D12.03; -.
DR   eggNOG; KOG0360; Eukaryota.
DR   HOGENOM; CLU_008891_7_3_1; -.
DR   InParanoid; O94501; -.
DR   OMA; KNYKNYG; -.
DR   PhylomeDB; O94501; -.
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:O94501; -.
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; 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; cd03335; TCP1_alpha; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012715; Chap_CCT_alpha.
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; TIGR02340; chap_CCT_alpha; 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..556
FT                   /note="T-complex protein 1 subunit alpha"
FT                   /id="PRO_0000128314"
SQ   SEQUENCE   556 AA;  60047 MW;  34DE8D22AA56D812 CRC64;
     MFQAPRESTL FLSGEKISGE DVRNQNVLAT TAIANVVKSS LGPVGLDKML VDDIGDVTVT
     NDGATILSLL DVEHPAGKVL VELAQQQDKE VGDGTTSVVI IAAELLRRAN ELVKNKIHPT
     TIITGYRLAI REAVKFMTDV LSCSVDSLGK ESLINVAKTS MSSKIIGNDS DFFSTMAVDA
     MLSVKTSNSK GETRYPVKAV NILKAHGKSS RESVLVKGYA LNCTIASQAM KTRVQNAKIA
     VLDMDLQKTK MALGVHVTID DPDQLEKIRE REVMITLERV KKILNAGANV ILTTKGIDDL
     CLKSIIEAGA MAVRRCKKED LRRIAKASGA TLLSSLSNLE GEETFESSYL GSAEEVVQEK
     FSDDECILVK GTKAYSSASI VLRGPNEYSL DEMERSMHDS LSVVKRTLES GKVVPGGGAV
     ETALSIYLEN FATSLGSREQ LAIAEFAQAL LIIPRTLAVN AAKDSTELTA KLRAYHAASQ
     NAEVTDVKKR GYKNYGLDLL NGVIRDNVKA GVLEPSMSKL KSLKSAVEAC IAILRIDTSI
     KLDPERQPED PHAGLH