ID   TCPD_CAEEL              Reviewed;         540 AA.
AC   P47208;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=cct-4; ORFNames=K01C8.10;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7576182; DOI=10.1089/dna.1995.14.951;
RA   Leroux M.R., Candido E.P.M.;
RT   "Characterization of four new tcp-1-related cct genes from the nematode
RT   Caenorhabditis elegans.";
RL   DNA Cell Biol. 14:951-960(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; U25697; AAA92842.1; -; mRNA.
DR   EMBL; Z49068; CAA88861.1; -; Genomic_DNA.
DR   PIR; T23173; T23173.
DR   RefSeq; NP_495750.1; NM_063349.6.
DR   AlphaFoldDB; P47208; -.
DR   SMR; P47208; -.
DR   BioGRID; 39659; 12.
DR   IntAct; P47208; 2.
DR   STRING; 6239.K01C8.10.2; -.
DR   EPD; P47208; -.
DR   PaxDb; P47208; -.
DR   PeptideAtlas; P47208; -.
DR   EnsemblMetazoa; K01C8.10.1; K01C8.10.1; WBGene00000379.
DR   EnsemblMetazoa; K01C8.10.2; K01C8.10.2; WBGene00000379.
DR   GeneID; 174330; -.
DR   KEGG; cel:CELE_K01C8.10; -.
DR   UCSC; K01C8.10.1; c. elegans.
DR   CTD; 174330; -.
DR   WormBase; K01C8.10; CE02262; WBGene00000379; cct-4.
DR   eggNOG; KOG0358; Eukaryota.
DR   GeneTree; ENSGT00550000074956; -.
DR   HOGENOM; CLU_008891_9_1_1; -.
DR   InParanoid; P47208; -.
DR   OMA; HPAANMI; -.
DR   OrthoDB; 511484at2759; -.
DR   PhylomeDB; P47208; -.
DR   BRENDA; 3.6.4.B10; 1045.
DR   Reactome; R-CEL-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-CEL-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P47208; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000379; Expressed in germ line (C elegans) and 4 other tissues.
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; ISS:WormBase.
DR   GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:WormBase.
DR   GO; GO:0006457; P:protein folding; ISS:WormBase.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..540
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000128337"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  58391 MW;  1AC61EA6CD0AA5CD CRC64;
     MPPAVPAAAA TARQSASGRE RNFKDKDKPE SVRNSNIVAA KAVADAVRTS LGPRGMDKMI
     QSGNGDVTIT NDGATILNQM SVIHPTAKML VELSKAQDIE AGDGTTTVVV MAGALLDAAQ
     NLLSKGIHPT TISESFQSAA AEAEKILDEM SSPVDLSNDA LLNKMATTSL NSKVVSQHSW
     LLAPMAVNAV KKIINSENDS NVNLKMIKII KKMGDTVEES ELIEGALIDQ KTMGRGAPTR
     IEKAKIGLIQ FQISPPKTDM ENQVIITDYA QMDRALKEER QYLLEICKQI KAAGCNVLLI
     QKSILRDAVN ELALHFLAKM KIMCIKDIER EDIEFYSRIL GCRPVASVDH FNADALGYAD
     LVEEIPTGGD GKVIKVTGVQ NPGHAVSILL RGSNKLVLEE ADRSIHDALC VIRCLVKKKA
     LLPGGGAPEM EIAVKLRNLA QTQHGATQYC WRAFADALEL IPYTLAENAG LSPIHTVTEL
     RNNHANGNSS YGVNVRKGYV TDMVEEDVVQ PLLVTASAIK QASECVRSIL KIDDIVMAVR