ID   TCPH_ENCCU              Reviewed;         511 AA.
AC   Q8SR53;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=T-complex protein 1 subunit eta;
DE            Short=TCP-1-eta;
DE   AltName: Full=CCT-eta;
GN   Name=CCT7; OrderedLocusNames=ECU10_0630;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the T-complex protein 1 (TCP1) complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AL590449; CAD25782.1; -; Genomic_DNA.
DR   RefSeq; NP_586178.1; NM_001042011.1.
DR   AlphaFoldDB; Q8SR53; -.
DR   SMR; Q8SR53; -.
DR   STRING; 284813.Q8SR53; -.
DR   GeneID; 859827; -.
DR   KEGG; ecu:ECU10_0630; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_0630; -.
DR   HOGENOM; CLU_008891_7_1_1; -.
DR   InParanoid; Q8SR53; -.
DR   OMA; HRKGNTW; -.
DR   OrthoDB; 335406at2759; -.
DR   Proteomes; UP000000819; Chromosome X.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IEA:UniProt.
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; IEA:InterPro.
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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..511
FT                   /note="T-complex protein 1 subunit eta"
FT                   /id="PRO_0000378558"
SQ   SEQUENCE   511 AA;  56262 MW;  5976DB0FFDF762A0 CRC64;
     MNQLFVQTEK IVDPREGKLQ VVSNVDVCTK IAEFLESTLG PYGMDKLFAG KEIVVTNDGA
     TILKHMNIRH PVGRLLVALS ESQDSEVGDG TTSVVILTTE ILSCLKPLIK DNFDLGCIKG
     CLEELRMMCI EHLEKMGMEL DDEVLYKLAG TCITSKNIRH EKEYFSRMIV DAVKQAKIDD
     AESIGVKKVQ GGSIGDSVAV NGIAFEKCFT YAGYEQQPKR ILNPRILCLN VELEWKSERD
     NAEIRVGGVE EYQRVVDAEW AIIRRKLDEI ISSGANVVLS SLSIGDYATQ YFAKHGIFCA
     GRVSKEDLGR VVGSCGGSIL GATDYLEGSL GACALFEERQ LGKFRYNYFE GGGTSACTMI
     LRGPGQEVLE EIGRSVHDAV CVVRTALRTR KVVTGGGSVE MELSRIIREK SMKYDDKRMF
     VAKAVGQAFE KIPLLLARNF GLDTISTIQD LRKRHANGDS CEGISIDGAR DMQKLGIYEP
     LEVKKNMVKA SFSAAASIIM IDSTIMAEKS Q