ID   TCPA_DICDI              Reviewed;         548 AA.
AC   Q55BM4; O76126;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=T-complex protein 1 subunit alpha;
DE            Short=TCP-1-alpha;
DE   AltName: Full=CCT-alpha;
DE   AltName: Full=DdTcp-1;
GN   Name=tcp1; ORFNames=DDB_G0269190;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=AX3-1;
RX   PubMed=9630545; DOI=10.1016/s0378-1119(98)00190-5;
RA   Iijima M., Shimizu H., Tanaka Y., Urushihara H.;
RT   "A Dictyostelium discoideum homologue to Tcp-1 is essential for growth and
RT   development.";
RL   Gene 213:101-106(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- DEVELOPMENTAL STAGE: Expressed in both sexually mature and immature
CC       cells at the growth phase. {ECO:0000269|PubMed:9630545}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AB008158; BAA32082.1; -; mRNA.
DR   EMBL; AAFI02000005; EAL71945.1; -; Genomic_DNA.
DR   PIR; T43895; T43895.
DR   RefSeq; XP_646807.1; XM_641715.1.
DR   AlphaFoldDB; Q55BM4; -.
DR   SMR; Q55BM4; -.
DR   STRING; 44689.DDB0191128; -.
DR   PaxDb; Q55BM4; -.
DR   EnsemblProtists; EAL71945; EAL71945; DDB_G0269190.
DR   GeneID; 8617780; -.
DR   KEGG; ddi:DDB_G0269190; -.
DR   dictyBase; DDB_G0269190; tcp1.
DR   eggNOG; KOG0360; Eukaryota.
DR   HOGENOM; CLU_008891_5_1_1; -.
DR   InParanoid; Q55BM4; -.
DR   OMA; KNYKNYG; -.
DR   PhylomeDB; Q55BM4; -.
DR   BRENDA; 3.6.4.B10; 1939.
DR   Reactome; R-DDI-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-DDI-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:Q55BM4; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; ISS:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
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; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
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..548
FT                   /note="T-complex protein 1 subunit alpha"
FT                   /id="PRO_0000327895"
FT   CONFLICT        247
FT                   /note="M -> L (in Ref. 1; BAA32082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="V -> I (in Ref. 1; BAA32082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="N -> T (in Ref. 1; BAA32082)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   548 AA;  59406 MW;  B286C36F0DDAB94B CRC64;
     MSNKVLMIDG DRISGNEVRA QNVLAVTAIA NIVKTSFGPI GLDKMLIDNI GSIVVTNDGA
     TILQKIDIEH PAAKILVQLS ELQDQEVGDG TTTVVILAAE LLKRANELVA RKVHPTVIIS
     GFRLACTEAI KYINETLAVK VETLPKDFIV NIAKTSMSSK TINDDSDFFS KIVIEAITRV
     KTIDYKGDVK YPINAINILK AHGKSAKEST LVEGYALNCT VASEGMPKRI QGAKIAFLDF
     NLAKTKMKLG QKVVVTNVND LEAIRDREND IVKERISLII KSGANVVLTT KGIDDLCLKY
     FVEAGCMAVR RCKKEDLKRI AKSCGGTVLI TLANLEGEES FDTTALGIAD EVVQDRLADD
     ELIIVKNSNK KSASIILRGA NELMLDEMER SIHDSLCIVK RTLESGTIVP GGGAVESALS
     IYLDNIAATM GSRKQLAISE FAESLLVVPK QLAVNAALDA SDLVSKLKAY HHAAQTDPSK
     KSYAYSGLDL FNNKVRNNLE AGVLEPAIAK IKCIKFATES AITILRIDDK ITLNPREQQG
     GDHEGHGH