ID   TCPD_CANGA              Reviewed;         529 AA.
AC   Q6FQT2;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=CCT4; OrderedLocusNames=CAGL0I03762g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380955; CAG60349.1; -; Genomic_DNA.
DR   RefSeq; XP_447412.1; XM_447412.1.
DR   AlphaFoldDB; Q6FQT2; -.
DR   SMR; Q6FQT2; -.
DR   STRING; 5478.XP_447412.1; -.
DR   EnsemblFungi; CAG60349; CAG60349; CAGL0I03762g.
DR   GeneID; 2889151; -.
DR   KEGG; cgr:CAGL0I03762g; -.
DR   CGD; CAL0130482; CAGL0I03762g.
DR   VEuPathDB; FungiDB:CAGL0I03762g; -.
DR   eggNOG; KOG0358; Eukaryota.
DR   HOGENOM; CLU_008891_9_1_1; -.
DR   InParanoid; Q6FQT2; -.
DR   OMA; HPAANMI; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IEA:EnsemblFungi.
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:EnsemblFungi.
DR   GO; GO:0051086; P:chaperone mediated protein folding independent of cofactor; IEA:EnsemblFungi.
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..529
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000128340"
SQ   SEQUENCE   529 AA;  57645 MW;  C7AE06D32C6016F8 CRC64;
     MVAQKSVSNA TFKNKEKPQE VRRANIVAAR AVADAIRTSL GPKGMDKMIK TSRGEIIISN
     DGHTILKQMA ILHPVAKMLV DVSAAQDSEA GDGTTSVVIL TGALLGAADR LLNKGIHPTI
     IAESFQKAAR RSVETLLEIC HPVSLDDRED LIRAASTSLS SKIVSQYSSF LSPLAVDAVL
     SITEKDSKTV DLNDIRLVKK VGGTIGDTEM VDGVVLTQTV VKTAGGPTMK EKAKIGLIQF
     QISPPKPDTE NNIVVSDYRQ MDKILKEERA YLLNICKKIK KAKCNVLLIQ KSILRDAVND
     LALHFLAKLG IMVIKDIERE EIEFLSKSLG CKPISDVELF TEDRLGSADL VEEIDSDGTK
     IVKFSGVKGV NAKPTVSVII RGANSMILDE TERSLHDALC VIRCLVKERG LIAGGGAPEI
     EISRRLERES RSMEGVEAYI WQEFAQALEV IPTTLAENAG LNSIKVITEL RSRHENGDVN
     EGISVRRSGT TNTYEEHILQ PVLVSTSAIT LASECVKSIL RIDDITFSR