TCPG_OXYGR
ID TCPG_OXYGR Reviewed; 559 AA.
AC O00782;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=T-complex protein 1 subunit gamma;
DE Short=TCP-1-gamma;
DE AltName: Full=CCT-gamma;
DE AltName: Full=Chaperonin subunit CCTV gamma;
OS Oxytricha granulifera (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=5947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O 5-1;
RX PubMed=9288910; DOI=10.1111/j.1432-1033.1997.00877.x;
RA Palmedo G., Ammermann D.;
RT "Cloning and characterization of the Oxytricha granulifera chaperonin
RT containing tailless complex polypeptide 1 gamma gene.";
RL Eur. J. Biochem. 247:877-883(1997).
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.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; Y11967; CAA72704.1; -; Genomic_DNA.
DR AlphaFoldDB; O00782; -.
DR SMR; O00782; -.
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.
DR PROSITE; PS00995; TCP1_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Disulfide bond; Nucleotide-binding.
FT CHAIN 1..559
FT /note="T-complex protein 1 subunit gamma"
FT /id="PRO_0000128328"
FT REGION 531..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 368..374
FT /evidence="ECO:0000250"
SQ SEQUENCE 559 AA; 61989 MW; 77056918F5514CB6 CRC64;
MSSRAAVFIL NQNAKREQGR KAQTANIKAA RAVSDIVRTT LGPKSMLKML LDPMGGIVLT
NDGNAILREI DVAHPAAKSM IELARAQDEE VGDGTTSVII LAGEILSAVE SFLERDIHPT
VIVGAYFQAL EEIVRLTESY GEPIDIENEN DLQKIVSSCI GTKFSSKWGN LIVDLAVKAV
KSVYKKEGDY VEIDVKRYAK VEKIPGGLLE ESVVLDGVMF NKDVTHPGMR RYIENPRVVL
LDCPLEYKKG ESMTNMEFTK EEDFKKALMM EEEEVKKMCA EDILRVKPDV VITEKGVSDT
AQHFLLKYGN CTVIRRIRKT DNNRIARVTG ATIANRPEEL QESDVGTKCG LFEIKKIGDE
YFSFMTKCEN PKACSILLRG ASKDVLNEIE RNLHDALGVA RNVMVNPKLV PGGGAIEMEL
ACRLMEFSQK IEGMQQWPFK ALAGALEVIP RTLAQNCGAD VVRVMTELRA KHANDKEGLY
WGIDGNTGKI RDMRESNVWD PISVKQQTLK TSIEATCMLL RIDDIVSGIK KDKRGGAGQR
GGDRGQGDQE ETFGDQRDG
