ID   TCPE_SCHPO              Reviewed;         546 AA.
AC   Q9UTM4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=T-complex protein 1 subunit epsilon;
DE            Short=TCP-1-epsilon;
DE   AltName: Full=CCT-epsilon;
GN   Name=cct5; ORFNames=SPAC1420.02c;
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; CAB57321.1; -; Genomic_DNA.
DR   PIR; T37665; T37665.
DR   RefSeq; NP_593277.1; NM_001018673.2.
DR   AlphaFoldDB; Q9UTM4; -.
DR   SMR; Q9UTM4; -.
DR   BioGRID; 279313; 5.
DR   STRING; 4896.SPAC1420.02c.1; -.
DR   MaxQB; Q9UTM4; -.
DR   PaxDb; Q9UTM4; -.
DR   PRIDE; Q9UTM4; -.
DR   EnsemblFungi; SPAC1420.02c.1; SPAC1420.02c.1:pep; SPAC1420.02c.
DR   GeneID; 2542868; -.
DR   KEGG; spo:SPAC1420.02c; -.
DR   PomBase; SPAC1420.02c; cct5.
DR   VEuPathDB; FungiDB:SPAC1420.02c; -.
DR   eggNOG; KOG0357; Eukaryota.
DR   HOGENOM; CLU_008891_7_2_1; -.
DR   InParanoid; Q9UTM4; -.
DR   OMA; QTGSNDM; -.
DR   PhylomeDB; Q9UTM4; -.
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:Q9UTM4; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005856; C:cytoskeleton; ISO: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; cd03339; TCP1_epsilon; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012718; Chap_CCT_epsi.
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; TIGR02343; chap_CCT_epsi; 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..546
FT                   /note="T-complex protein 1 subunit epsilon"
FT                   /id="PRO_0000128353"
SQ   SEQUENCE   546 AA;  59377 MW;  DAB279CF67BFDC94 CRC64;
     MAGLDNAVMV RDDQGNPFIL VRDQEKKRRL HGIDAVKSHI LATKTVANIV RTSLGPRGLD
     KILISPDGEI TVTNDGATIL DQMEVEHQIA KLLVQLSKSQ DDEIGDGTTG VVVLAGALLE
     QAEALIDKGI HPIRIADGYE KACQVAVKHL DAISDVVDFS PENTTNLFRS AKTSLGSKVV
     SKAHDHFANI AVDAVLSVAD LQRKDVDFEL IKVDGKVGGS VDDTKLVKGV VVDKDMSHPQ
     MPHRIENAKI AILTCPFEPP KPKTKHKLDI TSVSEFEALQ AYEKEKFQEM IKHVKDAGAN
     LVICQWGFDD EANHLLLQNN LPAVRWVGGP EIELIAIATN GRIVPRFEDL SSDKLGSAGI
     VREVSFGTTR DKILVIEKCA NSRAVTVFVR GSNKMIVDEA KRALHDALCV VRNLIRDNRV
     VYGGGAAEIS CSLAVTKEAE KIPGIDQYSM GAFADALDTI PLALAENSGL SSIEALTAVK
     ARHVKENKAY LGIDCLQTGS NDMRKQFVID PLIGKKQQLL LATQLCRMVL KVNDIIVAGS
     KDDDYN