ID   TCPD_SCHPO              Reviewed;         527 AA.
AC   P50999; O59929; Q9URV5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=cct4; ORFNames=SPBC106.06;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=972 / ATCC 24843;
RA   Mueller U.W., Sazer S.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
RC   STRAIN=972 / ATCC 24843;
RA   Rochet M., Levesque H., Gaillardin C.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
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; AF050465; AAC05213.1; -; mRNA.
DR   EMBL; CU329671; CAB53722.1; -; Genomic_DNA.
DR   EMBL; X91498; CAA62798.1; -; Genomic_DNA.
DR   PIR; T39263; T39263.
DR   PIR; T43649; T43649.
DR   RefSeq; NP_595155.1; NM_001021064.2.
DR   AlphaFoldDB; P50999; -.
DR   SMR; P50999; -.
DR   BioGRID; 276591; 10.
DR   IntAct; P50999; 2.
DR   STRING; 4896.SPBC106.06.1; -.
DR   iPTMnet; P50999; -.
DR   MaxQB; P50999; -.
DR   PaxDb; P50999; -.
DR   PRIDE; P50999; -.
DR   EnsemblFungi; SPBC106.06.1; SPBC106.06.1:pep; SPBC106.06.
DR   GeneID; 2540053; -.
DR   KEGG; spo:SPBC106.06; -.
DR   PomBase; SPBC106.06; cct4.
DR   VEuPathDB; FungiDB:SPBC106.06; -.
DR   eggNOG; KOG0358; Eukaryota.
DR   HOGENOM; CLU_008891_9_1_1; -.
DR   InParanoid; P50999; -.
DR   OMA; HPAANMI; -.
DR   PhylomeDB; P50999; -.
DR   Reactome; R-SPO-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-SPO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P50999; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IDA:PomBase.
DR   GO; GO:0005856; C:cytoskeleton; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
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; ISO:PomBase.
DR   GO; GO:0006457; P:protein folding; ISO:PomBase.
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..527
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000128343"
FT   CONFLICT        78
FT                   /note="L -> R (in Ref. 1; AAC05213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="Missing (in Ref. 1; AAC05213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="D -> EV (in Ref. 1; AAC05213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        440
FT                   /note="R -> G (in Ref. 1; AAC05213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        463..464
FT                   /note="QV -> RI (in Ref. 1; AAC05213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        470..481
FT                   /note="SRHANGEKTAGI -> KSYLREDCGY (in Ref. 1; AAC05213)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   527 AA;  56968 MW;  ACB5D86F9A83C02E CRC64;
     MSKAATVPVA FQDREKPQEV RLSNIMAARS VADAIRTSLG PKGMDKMIQT GKGEVILTND
     GATILKHLSV LHPAAKMLVD LSAAQDVEAG DGTTSVVILA GSMLACAEKL LKKGIHPTVI
     AESFQRAAGF TVDCMKENAL AIELSDRESL LRAATTSLNS KIVSQYSNLL APIAVDAVLK
     VIDPRVATNV DLKDIRIVKK LGGIIDDTEL IPGLALTQTA VKSAGGPTRI EKANIALIQF
     QLSPPKPDME NQVVVNDYRQ MDKILKEERQ YLLNMCKKIK KAGANVILIQ KSILRDAVND
     LALHFLAKLK IMVIKDIERD EVEFICKSTG CKPIADIESF AEDKLGHADL VEETSSSGEK
     IVKFSGVKNA GKTVSILCRG ANLLTLEEAE RSLHDALCVI RCLVKQRALI AGGGSPEIEA
     AQRLLEHARQ LEGREAICIR AFSEALEIIP VTLAENAGLN AIQVVTELRS RHANGEKTAG
     INVRKGIVTN ILEENVLQPL LVNISAIQLA AETTKMIMKI DDITLAR