ID   TCPD_YARLI              Reviewed;         527 AA.
AC   Q6C100;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=CCT4; OrderedLocusNames=YALI0F20416g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382132; CAG78471.1; -; Genomic_DNA.
DR   RefSeq; XP_505662.1; XM_505662.1.
DR   AlphaFoldDB; Q6C100; -.
DR   SMR; Q6C100; -.
DR   STRING; 4952.CAG78471; -.
DR   EnsemblFungi; CAG78471; CAG78471; YALI0_F20416g.
DR   GeneID; 2907866; -.
DR   KEGG; yli:YALI0F20416g; -.
DR   VEuPathDB; FungiDB:YALI0_F20416g; -.
DR   HOGENOM; CLU_008891_9_1_1; -.
DR   InParanoid; Q6C100; -.
DR   OMA; HPAANMI; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0051086; P:chaperone mediated protein folding independent of cofactor; IEA:EnsemblFungi.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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..527
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000128344"
SQ   SEQUENCE   527 AA;  56483 MW;  0C0A84CFCF179C1B CRC64;
     MSVPTGTKSG FKNKEKPLEV RKSNILAARA VADAIRTSLG PKGMDKMIQT ARGQVIISND
     GNTILQHMAV MHPAAKMLVD LSASQDSVAG DGTTSVVILA GSLLGAADKL LKKGIHPSII
     AENFQKAAQR AAEVVMDMSK PIDLSDRETL IRAASTSLNS KIVSQFSSTL APMLVDAALQ
     AAKKTPEGGL TLDLNDIRII KSLGGTIEDT TLANGLVLNN YAVKNAGGPS RMEKAKIGLI
     QFQLSAPKPD MENHIVVNDY RQMDKILKEE RQYILGLAKA IKKSKCNVLL IQKSILRDAV
     SELALHFLAK LNIMVIKDIE RDDIEFISRS TGAKPVADIE AFTEDKLGSC DLVEEVESSG
     SKTVRFSSRE GSNTVSILVR GANDLVIDET ERSLHDALCV LRSLFRVPAL VPGGGACEVQ
     VAQVIGKESR AMDGASAICY EEFSNAMLVI PTTLAENAGL NPVNVVTELR VRHEKGEVNA
     GISVRRGTSI MVEEHVIQPA LVTTSAITLA AECAKGLLRI DDIAFSR