ID   CH60_TRIVA              Reviewed;         470 AA.
AC   Q95058;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Hydrogenosomal chaperonin HSP60;
DE            Short=Protein Cpn60;
DE   AltName: Full=Heat shock protein 60;
DE   AltName: Full=groEL protein;
GN   Name=HSP60;
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8790385; DOI=10.1073/pnas.93.18.9651;
RA   Bui E.T., Bradley P.J., Johnson P.J.;
RT   "A common evolutionary origin for mitochondria and hydrogenosomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:9651-9656(1996).
CC   -!- FUNCTION: Implicated in hydrogenosomal protein import and
CC       macromolecular assembly. May facilitate the correct folding of imported
CC       proteins. May also prevent misfolding and promote the refolding and
CC       proper assembly of unfolded polypeptides generated under stress
CC       conditions in the hydrogenosome (Potential). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Hydrogenosome.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U26966; AAB17250.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q95058; -.
DR   SMR; Q95058; -.
DR   STRING; 5722.XP_001582336.1; -.
DR   VEuPathDB; TrichDB:TVAG_167250; -.
DR   eggNOG; KOG0356; Eukaryota.
DR   GO; GO:0042566; C:hydrogenosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   CDD; cd03344; GroEL; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Cpn60/GroEL.
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   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Hydrogenosome; Nucleotide-binding.
FT   CHAIN           1..470
FT                   /note="Hydrogenosomal chaperonin HSP60"
FT                   /id="PRO_0000063638"
SQ   SEQUENCE   470 AA;  50614 MW;  6D501801045605AF CRC64;
     MSLIEAAKHF TRAFAKARDL KFGSDARDHL LLGVEKLADA VVSTLGPKGR NVMIELPYGP
     PKVTKDGVTV AKSIEFKDKW QNLGAQLVIN VAQKTNDVAG DGTTTATLLT RELYRESIKA
     LSAGLDPNKV RKGMTLRVDA VVKELEKSTK KVSSPDEIFN VATISANGSE KIGHLIADAF
     KAVGNEGVIT VAMGKKFDHE LETVQGMKID RGYISSYFQN DTKSMKCEYE NPYILITDIK
     INSFAQIAPI LEKIITTGRP LLIIADDVEG DALATLIVNK IRGSLKVVAI RAPGFGDNKK
     NTLQDIAVAT GGQYISEELG LKLEEATQQM LGQCNKITVS KDDCIILGGA GDKDAMKARS
     EDIKKQLSNT QSKYETDKLR ERLAKLTGGV AVISVGGANE VEVGEEKDLI DDALNATRAA
     IEEGIVAGGG TALLRASAVL EPLKKDKGLE ERTGIEIIQN SHQTASHSHC