ID   TCPD_DEBHA              Reviewed;         533 AA.
AC   Q6BXF6;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=CCT4; OrderedLocusNames=DEHA2B03410g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; CR382134; CAG85104.1; -; Genomic_DNA.
DR   RefSeq; XP_457113.1; XM_457113.1.
DR   AlphaFoldDB; Q6BXF6; -.
DR   SMR; Q6BXF6; -.
DR   STRING; 4959.XP_457113.1; -.
DR   EnsemblFungi; CAG85104; CAG85104; DEHA2B03410g.
DR   GeneID; 2913124; -.
DR   KEGG; dha:DEHA2B03410g; -.
DR   VEuPathDB; FungiDB:DEHA2B03410g; -.
DR   eggNOG; KOG0358; Eukaryota.
DR   HOGENOM; CLU_008891_9_1_1; -.
DR   InParanoid; Q6BXF6; -.
DR   OMA; HPAANMI; -.
DR   OrthoDB; 511484at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
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   GO; GO:0051086; P:chaperone mediated protein folding independent of cofactor; IEA:UniProt.
DR   CDD; cd03338; TCP1_delta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012717; Chap_CCT_delta.
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; TIGR02342; chap_CCT_delta; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..533
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000128341"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  57629 MW;  A45257DA46914DC2 CRC64;
     MAQSQVGKGS PSNATFRDKE KPQEVRKSNI LAARAVSDAI RTSLGPKGMD KMIKTKNGEI
     IISNDGATIL KHMAVLHPAA RMLVDVSAAQ DVEAGDGTTS VAILTGSLLG AAEKLLNKGI
     HPTLISESFQ RAATRSAEVL LEMSHKISLD DKEALIRAAS TSLSSKIVSQ HSSLLSPLAV
     NSVLKVMNEE HTNVDLNDIR LIKKVGGTID ETELVNGVVL TQNVVKTAGG PVRVDKAKIA
     LIQFQLSPPK PDMENNVVVN DYRQMDKILK EERAYLLNIC KKIKKSKCNV LLIQKSILRD
     AVNDLALHFL SKLNIMVIKD IERDEIEFLS KATGCKPIAD IDNFTEDRLG SADVVEEIES
     SGSRIVKIDG VSAKNVKPTV SIVCRGANQL VLDETERSIH DALCVVRCLV KEKALIAGGG
     APEIEVSRVL MSEANKLSGV EQFVYQEFAQ ALEVIPTTLA ENAGLNSINV VTDLRNRHAN
     GEKNAGISVR RSGASNTYDE HVLQPVLVSS SAITLASECV KSILRIDDIA FSR