ID   TCPG_THAWE              Reviewed;         558 AA.
AC   Q9LKI7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=T-complex protein 1 subunit gamma;
DE            Short=TCP-1-gamma;
DE   AltName: Full=CCT-gamma;
OS   Thalassiosira weissflogii (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Conticribra.
OX   NCBI_TaxID=1577725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Armbrust V.;
RT   "Structural features of nuclear genes in the centric diatom Thalassiosira
RT   weissflogii (Bacillariophyceae).";
RL   Submitted (JUN-2000) 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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AF276909; AAF81907.1; -; mRNA.
DR   AlphaFoldDB; Q9LKI7; -.
DR   SMR; Q9LKI7; -.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IEA:UniProt.
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; IEA:InterPro.
DR   CDD; cd03337; TCP1_gamma; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012719; Chap_CCT_gamma.
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; TIGR02344; chap_CCT_gamma; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Disulfide bond; Nucleotide-binding.
FT   CHAIN           1..558
FT                   /note="T-complex protein 1 subunit gamma"
FT                   /id="PRO_0000128326"
FT   DISULFID        381..387
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   558 AA;  61672 MW;  B9CF889C4FCB92E0 CRC64;
     MANQGMGPIM VLNSKTQRST GRQAQLGNIQ AARAVADIIR STLGPRSMLK MLLDPMGGIV
     ITNDGNCILR EVDVSHPTAK SMIELSRAHD EEVGDGTTSV IILAGEMLIN AEPFVRTNIH
     PTIIVRGYNY ALQEALTICE EWALVVDVHD SERVKSLVQS CIGAKFSSRW NDIMIDMALK
     AVLTVSRESR TPSFTPEAND VYAQKMEVDI KRYAKVEKIP GGEISDCAVL SGVMFNKDVT
     HSKMRRRIEN PRILLLDTPL EYKKGESQTN VEITDEEDWN TLLKMEEEYV ENMCMEIIAF
     KPDIVITEKG VSDLAQHYFA KANITAFRRL RKTDNNRVAR ATGATIVSRT DEIRESDIGT
     GCGLFEMRKI GEEYFAFFEE CKDPKACTII LRGGSKDVLN EIERNLTDAM QVVRNVVFDP
     RLLPGGGATE MAVSVGLRKA GLKLEGIQQG PFLAVGDAME VIPRTLAQNC GVSVIRTVTQ
     LRAKHAAAYE DSETSGNGTF PKCNWGIDGT TGKLVDMEEF GVWEPFSVKV QTIKTAVESA
     CMILRIDDIV SGSKKKGY