TCPA_ENCCU
ID TCPA_ENCCU Reviewed; 540 AA.
AC Q8SSC9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, 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;
GN Name=TCP1; Synonyms=CCT1; OrderedLocusNames=ECU03_0220;
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; AL590443; CAD26168.1; -; Genomic_DNA.
DR RefSeq; NP_597533.1; NM_001040897.1.
DR AlphaFoldDB; Q8SSC9; -.
DR SMR; Q8SSC9; -.
DR STRING; 284813.Q8SSC9; -.
DR GeneID; 858695; -.
DR KEGG; ecu:ECU03_0220; -.
DR VEuPathDB; MicrosporidiaDB:ECU03_0220; -.
DR HOGENOM; CLU_008891_5_1_1; -.
DR InParanoid; Q8SSC9; -.
DR OMA; KNYKNYG; -.
DR OrthoDB; 335406at2759; -.
DR Proteomes; UP000000819; Chromosome III.
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 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; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..540
FT /note="T-complex protein 1 subunit alpha"
FT /id="PRO_0000378553"
SQ SEQUENCE 540 AA; 58211 MW; F6570663395DDF97 CRC64;
MNKEISTADI LSGGESYSGI SAVEKNAKAM MKVYNAIKTS FGPLGLDKMC VDSAGEVSIT
NDGATILQNM LIDDPAAKIL VDLATQQDHE VGDGTTSVVL IAVSLIEKGA KLIASGVHPS
VVVSGYKMAF NECVQFIKKS MSKSTLNLGS KALRNVVETS ISSKVISSES EVFCGIVIDA
LKCIESVDEN RKNMYPIEDI NILKHPGGSM KESFLHQGYA LNCSLASNFM KRQVKKPKIL
CIDFGLQKYK NPLTVSIVVD DPNKLEDIRK KELEITRRQI KTIIDSGANV VLTTRGIDDM
CTKLLVEADV VGIRRCKKED LLVIAKATGT SLVSSIADIS GADSISSLGF ADKFEVVQIG
EEECVLINGL KKKMASIILR GANCQLLDEM QRSVHDAVCV LKRTLESNSV VPGGGAVECA
LSLMLEKFAF TVNSKEHVAI HRYAESLLSI PKILSTNAGL DSNELVANLL SSQSREMANS
SGSKFLGIDV TSGKIQDNFE FGIIEPSVNK MKSLKAATEA AISILRINEV IILPPDQSKN