TCPE_YEAST
ID TCPE_YEAST Reviewed; 562 AA.
AC P40413; D6VWN5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=T-complex protein 1 subunit epsilon;
DE Short=TCP-1-epsilon;
DE AltName: Full=CCT-epsilon;
GN Name=CCT5; Synonyms=TCP5; OrderedLocusNames=YJR064W; ORFNames=J1752;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YPH501;
RA Kim S.;
RT "Cytosolic chaperonin(CCT) subunits have a conserved ATPase domain but
RT diverged polypeptide-binding domains.";
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
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. In yeast may play a role in mitotic spindle formation.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA53132.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L37350; AAA53132.1; ALT_INIT; Genomic_DNA.
DR EMBL; L47993; AAB39290.1; -; Genomic_DNA.
DR EMBL; Z49564; CAA89592.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08851.1; -; Genomic_DNA.
DR PIR; S57083; S57083.
DR RefSeq; NP_012598.1; NM_001181722.1.
DR PDB; 4V81; X-ray; 3.80 A; E/M/e/m=1-562.
DR PDB; 4V8R; X-ray; 3.80 A; AE/Ae/BE/Be=1-562.
DR PDB; 4V94; X-ray; 3.80 A; E/M/e/m=1-562.
DR PDB; 5GW4; EM; 4.70 A; E/e=1-562.
DR PDB; 5GW5; EM; 4.60 A; E/e=1-562.
DR PDB; 6KRD; EM; 4.38 A; E/e=1-562.
DR PDB; 6KRE; EM; 4.45 A; E/e=1-562.
DR PDB; 6KS6; EM; 2.99 A; E/e=1-562.
DR PDB; 6KS8; EM; 4.69 A; E/e=1-562.
DR PDBsum; 4V81; -.
DR PDBsum; 4V8R; -.
DR PDBsum; 4V94; -.
DR PDBsum; 5GW4; -.
DR PDBsum; 5GW5; -.
DR PDBsum; 6KRD; -.
DR PDBsum; 6KRE; -.
DR PDBsum; 6KS6; -.
DR PDBsum; 6KS8; -.
DR AlphaFoldDB; P40413; -.
DR SMR; P40413; -.
DR BioGRID; 33821; 230.
DR ComplexPortal; CPX-2156; Chaperonin-containing T-complex.
DR DIP; DIP-2205N; -.
DR IntAct; P40413; 29.
DR MINT; P40413; -.
DR STRING; 4932.YJR064W; -.
DR iPTMnet; P40413; -.
DR MaxQB; P40413; -.
DR PaxDb; P40413; -.
DR PRIDE; P40413; -.
DR DNASU; 853527; -.
DR EnsemblFungi; YJR064W_mRNA; YJR064W; YJR064W.
DR GeneID; 853527; -.
DR KEGG; sce:YJR064W; -.
DR SGD; S000003825; CCT5.
DR VEuPathDB; FungiDB:YJR064W; -.
DR eggNOG; KOG0357; Eukaryota.
DR GeneTree; ENSGT00550000074988; -.
DR HOGENOM; CLU_008891_7_2_1; -.
DR InParanoid; P40413; -.
DR OMA; QTGSNDM; -.
DR BioCyc; YEAST:G3O-31697-MON; -.
DR BRENDA; 3.6.4.B10; 984.
DR Reactome; R-SCE-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-SCE-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR PRO; PR:P40413; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40413; protein.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0051086; P:chaperone mediated protein folding independent of cofactor; IDA:ComplexPortal.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
DR CDD; cd03339; TCP1_epsilon; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012718; Chap_CCT_epsi.
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; TIGR02343; chap_CCT_epsi; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..562
FT /note="T-complex protein 1 subunit epsilon"
FT /id="PRO_0000128354"
FT CONFLICT 3
FT /note="A -> T (in Ref. 1; AAA53132)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="R -> T (in Ref. 1; AAA53132)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="A -> D (in Ref. 1; AAA53132)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="S -> T (in Ref. 1; AAA53132)"
FT /evidence="ECO:0000305"
FT CONFLICT 274..279
FT /note="CPFEPP -> VHLNLL (in Ref. 1; AAA53132)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="L -> I (in Ref. 1; AAA53132)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="G -> N (in Ref. 1; AAA53132)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 44..62
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 143..163
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 291..316
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 413..435
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 445..461
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 466..476
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 478..486
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 491..504
FT /evidence="ECO:0007829|PDB:6KS6"
FT TURN 523..526
FT /evidence="ECO:0007829|PDB:6KS6"
FT HELIX 531..549
FT /evidence="ECO:0007829|PDB:6KS6"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:6KS6"
SQ SEQUENCE 562 AA; 61914 MW; 8CDAF88C6403655F CRC64;
MAARPQQPPM EMPDLSNAIV AQDEMGRPFI IVKDQGNKKR QHGLEAKKSH ILAARSVASI
IKTSLGPRGL DKILISPDGE ITITNDGATI LSQMELDNEI AKLLVQLSKS QDDEIGDGTT
GVVVLASALL DQALELIQKG IHPIKIANGF DEAAKLAISK LEETCDDISA SNDELFRDFL
LRAAKTSLGS KIVSKDHDRF AEMAVEAVIN VMDKDRKDVD FDLIKMQGRV GGSISDSKLI
NGVILDKDFS HPQMPKCVLP KEGSDGVKLA ILTCPFEPPK PKTKHKLDIS SVEEYQKLQT
YEQDKFKEMI DDVKKAGADV VICQWGFDDE ANHLLLQNDL PAVRWVGGQE LEHIAISTNG
RIVPRFQDLS KDKLGTCSRI YEQEFGTTKD RMLIIEQSKE TKTVTCFVRG SNKMIVDEAE
RALHDSLCVV RNLVKDSRVV YGGGAAEVTM SLAVSEEADK QRGIDQYAFR GFAQALDTIP
MTLAENSGLD PIGTLSTLKS KQLKEKISNI GVDCLGYGSN DMKELFVVDP FIGKKQQILL
ATQLCRMILK IDNVIISGKD EY
