ID   TCPA_PALPA              Reviewed;         559 AA.
AC   Q9W790;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=T-complex protein 1 subunit alpha;
DE            Short=TCP-1-alpha;
DE   AltName: Full=CCT-alpha;
GN   Name=TCP1; Synonyms=CCT1;
OS   Paleosuchus palpebrosus (Cuvier's smooth-fronted caiman) (Dwarf caiman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Caimaninae;
OC   Paleosuchus.
OX   NCBI_TaxID=84099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10353914; DOI=10.1093/genetics/152.2.743;
RA   Shintani S., O'Huigin C., Toyosawa S., Michalova V., Klein J.;
RT   "Origin of gene overlap: the case of TCP1 and ACAT2.";
RL   Genetics 152:743-754(1999).
CC   -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a
CC       molecular chaperone complex that assists the folding of proteins upon
CC       ATP hydrolysis. {ECO:0000250|UniProtKB:P17987}.
CC   -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC       heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC       rings, 12 to 16 nm in diameter. {ECO:0000250|UniProtKB:P17987}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P17987}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AF143496; AAD34972.1; -; mRNA.
DR   AlphaFoldDB; Q9W790; -.
DR   SMR; Q9W790; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; cd03335; TCP1_alpha; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012715; Chap_CCT_alpha.
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; TIGR02340; chap_CCT_alpha; 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.
FT   CHAIN           1..559
FT                   /note="T-complex protein 1 subunit alpha"
FT                   /id="PRO_0000128307"
SQ   SEQUENCE   559 AA;  60385 MW;  64F99F5045D1FA83 CRC64;
     MAALEGPLAV LGERSSGDTV RNQNVTAAAT IANIVKSSLG PVGLDKMLVD DIGDVTITND
     GATILKLLEV EHPAAKVLCE LAELQDKEVG DGTTSVVIIA AELLKNSDEL VKQKIHPTSI
     IGGYRLACKE AVRYINENLI INTDELGRDC LINSAKTSMS SKIIGIDGDF FASMVVDAAS
     AVKYTDQKGQ ARYPINSINV LKAHGRSQKE SILVNGYALN CVVGSQGMTK RIVNAKIACL
     DFSLQKTKMK LGVQVVITDP EKLDQIRQRE SDITKERIQK ILATGANVIL TTGGIDDMCL
     KYFVDAGAMA VRRVLKKDLK RIAKASGATV CSTLANLEGE ESFEASMLGQ AEEVVQERVC
     DDELILIKNT KARTSASIIL RGANDFMCDE MERSIHDALC VVKRVLESKS VVPGGGAVEA
     ALSIYLENYA TSMGSREQLA IAEFARSLLI IPNTLAVNAA QDATDLVAKL RAFHNEAQVN
     PERKNLKWIG LDLINGKPRD NKQAGVFEPT LVKTKSLKFA TEAAITILRI DDLIKLHPES
     KDDKGGCYED AVRSGALEE