ID   TCPD_ASHGO              Reviewed;         529 AA.
AC   Q75A36;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=CCT4; OrderedLocusNames=ADR083W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52003.1; -; Genomic_DNA.
DR   RefSeq; NP_984179.1; NM_209532.1.
DR   AlphaFoldDB; Q75A36; -.
DR   SMR; Q75A36; -.
DR   STRING; 33169.AAS52003; -.
DR   EnsemblFungi; AAS52003; AAS52003; AGOS_ADR083W.
DR   GeneID; 4620328; -.
DR   KEGG; ago:AGOS_ADR083W; -.
DR   eggNOG; KOG0358; Eukaryota.
DR   HOGENOM; CLU_008891_9_1_1; -.
DR   InParanoid; Q75A36; -.
DR   OMA; HPAANMI; -.
DR   Proteomes; UP000000591; Chromosome IV.
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..529
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000128339"
SQ   SEQUENCE   529 AA;  57361 MW;  94C0E7699C689337 CRC64;
     MPPKVSASNA TFKNREKPQE VRKANIIAAR AVADAIRTSL GPKGMDKMIK TARGEILISN
     DGHTILKQMA ILHPVAKMLV EVSAAQDSEA GDGTTSVVIL TGALLGAAEK LLAKGIHPTI
     IAESFQRAGQ RAVEVLLGMS KRISLQDRAE LVRAASTSLS SKIVSQYSTF LAPLAVDCVL
     SLTNEASTNV DLNDIRLVKK VGGTIDDTEM VDGVVLTQNI VKSAGGPVRM EKAKIGLIQF
     QISPPKPDTE NNIVVNDYRQ MDKILKEERA YLLKICKKIK KAKCNVLLIQ KSILRDAVNE
     LALHFLSKLN IVVIKDVERD EIEFLSKSLG CKPISDVELF TEDRLGSADL VEEIDSDGTK
     IVKITGIKTG NAKPTVSCIV RGANNVVLDE TERSLHDALC VIRCLVKERA LIAGGGAPEI
     EVSRTIMRES RAMQGVEAFV WQEFAEALEV IPTTLAENAG LNSIKVVTEL RSRHESGETN
     AGISVRRSGT TNTYDEHILQ PVLVSTSAIT LAAECVKSIL RIDDITFSR