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