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TCPQ_ENCCU
ID   TCPQ_ENCCU              Reviewed;         485 AA.
AC   Q8SS33;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=T-complex protein 1 subunit theta;
DE            Short=TCP-1-theta;
DE   AltName: Full=CCT-theta;
GN   Name=CCT8; OrderedLocusNames=ECU04_1020;
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; AL590444; CAD25290.1; -; Genomic_DNA.
DR   RefSeq; NP_584786.1; NM_001041136.1.
DR   AlphaFoldDB; Q8SS33; -.
DR   SMR; Q8SS33; -.
DR   STRING; 284813.Q8SS33; -.
DR   GeneID; 858934; -.
DR   KEGG; ecu:ECU04_1020; -.
DR   VEuPathDB; MicrosporidiaDB:ECU04_1020; -.
DR   HOGENOM; CLU_008891_4_3_1; -.
DR   InParanoid; Q8SS33; -.
DR   OMA; QYGILEF; -.
DR   OrthoDB; 617040at2759; -.
DR   Proteomes; UP000000819; Chromosome IV.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR017998; Chaperone_TCP-1.
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.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..485
FT                   /note="T-complex protein 1 subunit theta"
FT                   /id="PRO_0000378559"
SQ   SEQUENCE   485 AA;  53952 MW;  B0B4E6518D42DDCC CRC64;
     MDIGQTHLGG LISNSQQDEK VRYHIVGSRV RMACNLVKSL YGGSHRSKLI VNGYGQILLS
     SQPGVIYDNV KVNHPLVKLL QEYVKKMDVI GDGATFFVVL VSELIQEAID VIGRGMKPAC
     FSSLLREAHK EIDDLGRELL VEHRIDFEDK ESISMVLRGV LKDKWLEEIV VEGISLARSF
     SSESIRVCKV ACGSVEDSYV VEGMVFNRLP EGEVKHARQG RTSIYNCPLD ISRTELKGTV
     LMRTASELLS FSKEENKRIK ELVESIGADV IICSGKVDKI YLDFLNKGRK LVFRITSKYD
     LRRIRELLGG HILSTLEPPA EGSMGVVSEV ATFREGSTEY TKFISGSKKV YTLVLKNSVQ
     AVLDEHERMV QKALVVLSKN VSGGKIGLVD GAGRFERRLS KAFLERSAGL SGGKSLAYKC
     IGKALGTFGS SDVEVYDIYN AKIKALKYSM EFVSTLFETS DYLIGRPEAL NIGPRNNQHW
     DEEDH
 
 
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