ID   TCPA_SCHMA              Reviewed;         545 AA.
AC   Q94757;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=T-complex protein 1 subunit alpha;
DE            Short=TCP-1-alpha;
DE   AltName: Full=CCT-alpha;
GN   Name=TCP-1A;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Egyptian;
RA   Campos E.G., Hamdan F.F., Ribeiro P., Prichard R.K.;
RL   Submitted (AUG-1996) 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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; U55769; AAA99815.1; -; mRNA.
DR   AlphaFoldDB; Q94757; -.
DR   SMR; Q94757; -.
DR   STRING; 6183.Smp_017360.1; -.
DR   eggNOG; KOG0360; Eukaryota.
DR   HOGENOM; CLU_008891_5_1_1; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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; Reference proteome.
FT   CHAIN           1..545
FT                   /note="T-complex protein 1 subunit alpha"
FT                   /id="PRO_0000128311"
SQ   SEQUENCE   545 AA;  59440 MW;  992CCA919389E42C CRC64;
     MLTLGGERTS GESVRKQNVL AACSFANFVK TSLGPVGLDK MLVDDVGDVT ITNDGATILK
     LLDVEHPAAK ILVQLAQLQD EEVGDGTTSV VILAAALLKN ADELISRFVH PTTVINGYRL
     ACREACKYIQ EHMAYDVNKL GKAGLINVAR TAMSSKLINL DADMFSQMAV DALMAVEVSG
     GPKGPVYPIK AVNILKAHGR SMSESMLIDG YALNCTAASQ QMPRIIKKAK IAFLDFSLQK
     VKMKLGVQVV VKDPAQLEAI RQREADITKE RIQKILNAGA NVILTTGGID DLCMKYFVEV
     NAMAVRRCKK VDLKNMAKAT GGQLIVSLAD MEGDEVFDPT KLGNAEEVSQ ERICDDELII
     LRGPKVHPSA SIILRGANDF YVDEMERSLH DALLVVKRVL ESKRIVPGAG ACETAVSIYL
     ENYALTLSSR EQLAIAEFAR AMLSIPKQLA VNAGVDSTEL VARLRSCHNS SQSKPDQAHN
     KWWGLDLNNQ YVADCKEIGV FEPLVSKIKS LKFATEAAIT ILRIDDLIKL KEEKQPDHDG
     DECGY