TCPB_ENCCU
ID TCPB_ENCCU Reviewed; 508 AA.
AC Q8SQP2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=T-complex protein 1 subunit beta;
DE Short=TCP-1-beta;
DE AltName: Full=CCT-beta;
GN Name=CCT2; OrderedLocusNames=ECU09_0480;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC hydrolysis. {ECO:0000250}.
CC -!- SUBUNIT: Component of the T-complex protein 1 (TCP1) complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; AL590451; CAD27020.1; -; Genomic_DNA.
DR RefSeq; XP_955601.1; XM_950508.1.
DR AlphaFoldDB; Q8SQP2; -.
DR SMR; Q8SQP2; -.
DR STRING; 284813.Q8SQP2; -.
DR GeneID; 860386; -.
DR KEGG; ecu:ECU09_0480; -.
DR VEuPathDB; MicrosporidiaDB:ECU09_0480; -.
DR HOGENOM; CLU_008891_6_2_1; -.
DR InParanoid; Q8SQP2; -.
DR OMA; YCTGGEI; -.
DR OrthoDB; 335406at2759; -.
DR Proteomes; UP000000819; Chromosome IX.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:InterPro.
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; cd03336; TCP1_beta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012716; Chap_CCT_beta.
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 PANTHER; PTHR11353:SF23; PTHR11353:SF23; 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; TIGR02341; chap_CCT_beta; 1.
DR PROSITE; PS00750; TCP1_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..508
FT /note="T-complex protein 1 subunit beta"
FT /id="PRO_0000378554"
SQ SEQUENCE 508 AA; 55671 MW; 6E3C19118F21C295 CRC64;
MNIFSHANLG TTEERGDDAK RTILAGTDIV GDILKTTLGP KGMLKMLKGQ HVNVTNDGAF
ILNNLMIDSP SARILIGSST GQDWEEGDGT TSVAILASLL VKEAGKLEMH PTKILRGYRM
AQAKCEEILS SISFEATKED LLKLVRTTLC SKVLRYDLER FCEICVNAVE KLEGRNDLNL
IQIIKCSGKL EDSYLDDGFL LKKDIRIDDV VNPRVLIANT SMDQDKIKVF GAKINVNSVG
ELEEMEKAEK IKIKGKVERI SQNGVNVFVN RQLVYDYPLQ LLRMKGIQAI EHADFDGVER
LNNVLGGKIL STFDNMDESC YGTCESIRNV HVGNERMIKF SGVRSGASTI VLCGSSKEML
DEAERSVHDA LCVLAKIKED PRVIYGGGSS EMAMAVGLNK YAMEVPGAES DAILAFSSAL
QQIPKILADN GGYNGESIKA SLRAEHNSGR TSYGVNVRNG SIGCMKEAGV VDSLRIKHRV
VTAASETAQM IIKCDAIVKC KPRERTRE