ID   TCPD_ENCCU              Reviewed;         484 AA.
AC   Q8SSH3;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=CCT4; OrderedLocusNames=ECU02_0520;
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; AL590442; CAD25083.1; -; Genomic_DNA.
DR   RefSeq; NP_584579.1; NM_001040768.1.
DR   AlphaFoldDB; Q8SSH3; -.
DR   SMR; Q8SSH3; -.
DR   STRING; 284813.Q8SSH3; -.
DR   GeneID; 858569; -.
DR   KEGG; ecu:ECU02_0520; -.
DR   VEuPathDB; MicrosporidiaDB:ECU02_0520; -.
DR   HOGENOM; CLU_008891_9_2_1; -.
DR   InParanoid; Q8SSH3; -.
DR   OMA; HPAANMI; -.
DR   OrthoDB; 511484at2759; -.
DR   Proteomes; UP000000819; Chromosome II.
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..484
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000378556"
SQ   SEQUENCE   484 AA;  52842 MW;  66855B5501D44FA4 CRC64;
     MATERLNQVR TSVFQASQSL LQTLSTSLGP RGLDKMVVKD KKTVVTNDGA TILKYLNHHP
     IHGILSSMSA TQDEECGDGT TSVVILAGCL LESISSLLER NVHPSVICDN LEIAKKIGLR
     YIDRVKMECS EKDLISNVTT ALCSKIASST GEMAVEAIRG MEYVNGDKKN IRVVKKIGGN
     LDDVKAYKSI LLECDLKDIP KKAKVGVIQF CLSAPKTNMD SKILINDPAL MEKIIQDERK
     YILEMCKKIK KSGCTLLVVQ KSILRESLSD LASHFLKQLN ILVVNSVDRK DVDYICSAMN
     IQPVSEVDLL SPASLVDVET GEVEGMLEIK GYGCTILLRG CDDMVVEEAE RSLNDALCVV
     KCLKELPFLV PGGGSIEMGI ALMLSESTEG NIYVLREIAK AFEGVPYFLA RNAGLYPVEI
     VSELRSELKQ NCCAGISVRS GHAGDMVRDD SVVQPAKVSI SVVTLALETV SMILKIDDIL
     PARR