ID   TCPE_DICDI              Reviewed;         538 AA.
AC   Q54TD3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=T-complex protein 1 subunit epsilon;
DE            Short=TCP-1-epsilon;
DE   AltName: Full=CCT-epsilon;
GN   Name=cct5; ORFNames=DDB_G0281849;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000043; EAL66484.1; -; Genomic_DNA.
DR   RefSeq; XP_640456.1; XM_635364.1.
DR   AlphaFoldDB; Q54TD3; -.
DR   SMR; Q54TD3; -.
DR   STRING; 44689.DDB0233994; -.
DR   PaxDb; Q54TD3; -.
DR   EnsemblProtists; EAL66484; EAL66484; DDB_G0281849.
DR   GeneID; 8623269; -.
DR   KEGG; ddi:DDB_G0281849; -.
DR   dictyBase; DDB_G0281849; cct5.
DR   eggNOG; KOG0357; Eukaryota.
DR   HOGENOM; CLU_008891_7_2_1; -.
DR   InParanoid; Q54TD3; -.
DR   OMA; QTGSNDM; -.
DR   PhylomeDB; Q54TD3; -.
DR   BRENDA; 3.6.4.B10; 1939.
DR   Reactome; R-DDI-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-DDI-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:Q54TD3; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; ISS:dictyBase.
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; ISS:dictyBase.
DR   GO; GO:0006457; P:protein folding; ISS:dictyBase.
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..538
FT                   /note="T-complex protein 1 subunit epsilon"
FT                   /id="PRO_0000327897"
SQ   SEQUENCE   538 AA;  59130 MW;  16DF24F89FA96160 CRC64;
     MSLVFDEYGN PFIVIRDQQA KERLRGIEAH RSHILAAKTI SNIMKSSLGP KGMDKMMVSQ
     DGEVLVTNDG ATILENMQVD NQIAKLMVQL SKSQDDEIGD GTTGVVVLAG SLLEQAEQLI
     EKGIHPCRIY EGYETACKIA TEHLKTISDS IEFSKDNIEP LIKTAMTCLG SKIVNRFHRQ
     MSEIAVKAVI SVADLERKDV NLENIKLEGK EGGKLEDTQL VKGIIIDKGI SHPQMPKIIK
     DAKICLLTCP FEPPKPKTKN SIEITKAEDF KVLGEIEQKY FTDMVEKVKA TGANLVICQW
     GFDDEANHLL LQNNLPAVRW VGGLDLEKIA MATGGRIVAR FEDVSADKLG RAGLVREVGF
     GTTQDRYLSI EDCPNTNAVT IFVRGGNKMI VEEAKRSIHD ALCVTRNLIR DNRVIYGGGS
     SEISCGLKIS AMADDIASIE QYAVRAFADA LDAIPLALAE NSGLPSIESL STVKAMQIKE
     KNPRLGIDCN HRDTNDMKAQ HVFDTLPGKT QQFLLANQVV KMILKIDDII KMGPGADE