ID   TCPH_DICDI              Reviewed;         555 AA.
AC   Q54ER7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=T-complex protein 1 subunit eta;
DE            Short=TCP-1-eta;
DE   AltName: Full=CCT-eta;
GN   Name=cct7; ORFNames=DDB_G0291225;
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}.
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DR   EMBL; AAFI02000177; EAL61596.1; -; Genomic_DNA.
DR   RefSeq; XP_635173.1; XM_630081.1.
DR   AlphaFoldDB; Q54ER7; -.
DR   SMR; Q54ER7; -.
DR   STRING; 44689.DDB0191096; -.
DR   PaxDb; Q54ER7; -.
DR   PRIDE; Q54ER7; -.
DR   EnsemblProtists; EAL61596; EAL61596; DDB_G0291225.
DR   GeneID; 8628119; -.
DR   KEGG; ddi:DDB_G0291225; -.
DR   dictyBase; DDB_G0291225; cct7.
DR   eggNOG; KOG0361; Eukaryota.
DR   HOGENOM; CLU_008891_7_1_1; -.
DR   InParanoid; Q54ER7; -.
DR   OMA; HRKGNTW; -.
DR   PhylomeDB; Q54ER7; -.
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   Reactome; R-DDI-9013418; RHOBTB2 GTPase cycle.
DR   Reactome; R-DDI-9013422; RHOBTB1 GTPase cycle.
DR   PRO; PR:Q54ER7; -.
DR   Proteomes; UP000002195; Chromosome 6.
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; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03340; TCP1_eta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012720; Chap_CCT_eta.
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:SF22; PTHR11353:SF22; 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; TIGR02345; chap_CCT_eta; 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..555
FT                   /note="T-complex protein 1 subunit eta"
FT                   /id="PRO_0000327899"
SQ   SEQUENCE   555 AA;  60981 MW;  E0785F570BA8F327 CRC64;
     MSQMIRPPIV LLKEGTDTSQ GLPQLISNIN ACCAIVDTVR TTLGPRGMDK LIYQSERQVT
     ISNDGATVMK LLDIVHPAAR TLVDIAKSQD SEVGDGTTSV VILAGEFLKA AKPFLEEGIH
     PQIIIRAFRS ACELAKQKIQ ELSVDIKPEN MREFLEKCAS TSMNSKLIAS HKQFFSKMVV
     DAVQLLDDNI DLDMIGIKKE SGGGLGDSQF IAGAAFKRTF FYAGFEQQPK HIKNPKVLCL
     NIELELKAEK DNAEIRISDP TKYQSLVNAE WKLFFDKLEA IHASGVNVVL SKLAIGDLAT
     QFFADKNMFC AGRVPDDDIR RVCRATGAAI QNTTSNIIPD VIGTCDLFEE VQVGGQRYNL
     FTGCTMTQTA TIILRGGGEQ FIDEAERSLH DSIMIVRRAR KHRSVVAGGG AIEMEVSKYL
     RDYSLSIEGK KQLLINAFAK ALEVIPRQIA DNAGFDSTDI LNQLRQKHAQ GEKWFGVDIV
     NEGICDTYES AIWEPSLVKL NSIVAATEAT CLILSVDETV QNNQAEQAQA GPQINNQTRQ
     ALSRGRGVQA MRGRG