TCPE_ENCCU
ID TCPE_ENCCU Reviewed; 532 AA.
AC Q8SRP9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=T-complex protein 1 subunit epsilon;
DE Short=TCP-1-epsilon;
DE AltName: Full=CCT-epsilon;
GN Name=CCT5; OrderedLocusNames=ECU06_0990;
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; AL590446; CAD25459.1; -; Genomic_DNA.
DR RefSeq; NP_585855.1; NM_001041477.1.
DR AlphaFoldDB; Q8SRP9; -.
DR SMR; Q8SRP9; -.
DR STRING; 284813.Q8SRP9; -.
DR GeneID; 859280; -.
DR KEGG; ecu:ECU06_0990; -.
DR VEuPathDB; MicrosporidiaDB:ECU06_0990; -.
DR HOGENOM; CLU_008891_7_2_1; -.
DR InParanoid; Q8SRP9; -.
DR OMA; QTGSNDM; -.
DR OrthoDB; 511484at2759; -.
DR Proteomes; UP000000819; Chromosome VI.
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 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; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..532
FT /note="T-complex protein 1 subunit epsilon"
FT /id="PRO_0000378557"
SQ SEQUENCE 532 AA; 58417 MW; ABFAB37D091C9882 CRC64;
MSDLLTDELG QAFQITDEDK GCRIKGQQCI LANIGVVRSI ATFLSTSLGP TGMDKILQSK
DEDIVVTNDG ATILKEMEMT ENPISRLIVQ LSESQDEEIG DGTTSVVVLA SALLDQAQAL
LGQGVHPIKI SEGFEVGLGH AVEHLSEISE EISDLKETMM KAAKTSLGSK IVYKSLERFA
EICTDAVLMV ADMERKDLDF ELINIESKVG RDLSSTALIK GIVINKEFSH PQMKKEVKDG
RIALLSCPFE PPKLKTKHSL VISNPKEYKE LEEYEKKKFA EMIESIKRSG SNIVMCQWGF
DDEANSLLME NGLPAVRWVG GHELELLAVH TGGSIVARFE DLEESDLGKA RVREESLGTE
NDKIIVVENE GCSKAVTILV RGANDLVIEE AKRSIRDALC AVRNILTNSR IVYGGGSSEM
SCSLALERIA TGYSGEEREA ILGFGRALEE IPLCLARNSG HDPIGYSSDL RKLQMESKNF
HLGVDCLGDG EQDMKKLGVF DALSSKIRQF QMATQLVTMV LKIDNVVSDF HD