ID   CH60_EUGGR              Reviewed;         569 AA.
AC   Q39727; Q39723;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Chaperonin CPN60, mitochondrial;
DE   AltName: Full=HSP 60;
DE   Flags: Precursor;
GN   Name=HSP60;
OS   Euglena gracilis.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=W10BSML;
RA   Yasuhira S., Simpson L.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Z / UTEX 753;
RA   Siegner A.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Implicated in mitochondrial protein import and macromolecular
CC       assembly. May facilitate the correct folding of imported proteins. May
CC       also prevent misfolding and promote the refolding and proper assembly
CC       of unfolded polypeptides generated under stress conditions in the
CC       mitochondrial matrix.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; U49053; AAB03571.1; -; mRNA.
DR   EMBL; X95992; CAA65238.1; -; mRNA.
DR   AlphaFoldDB; Q39727; -.
DR   SMR; Q39727; -.
DR   GO; GO:0005739; C:mitochondrion; 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   HAMAP; MF_00600; CH60; 1.
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.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding; Stress response;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..569
FT                   /note="Chaperonin CPN60, mitochondrial"
FT                   /id="PRO_0000005013"
FT   CONFLICT        111
FT                   /note="T -> A (in Ref. 2; CAA65238)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   569 AA;  59707 MW;  BE935D4EE68ECF36 CRC64;
     MNRAGVLARR GYSSKGKDIL FGVDARVKML AGVNRLSQAV SVTLGPKGRN VVIEQPFGAP
     KITKDGVTVA KAIEFKDSFE NLGAQLVRQV ANTTNEIAGD GTTTSTVLAN TIFSEGYKAV
     TQGTSPVDMK RGIDRAVEVV LQSLTEQSKT IVSKEEVTQV ATISANGDVE IGQLIGHAME
     KVGKAGVITV SDGKTLDTEL EVVEGMSLDR GYISPYFVTN AKTQKVEIED AFILLCQKKV
     STIQQILPVL EHIAKANRPL VIIADDVDSE ALATLIINKI NGKLKVCAVK APGFGDNKTN
     MLHDVAIFTG GEVYNEELGM NLEQHFDHRI LGFAKKVSVG KDQTIILNGA GDPKAVEERK
     ELIQGMLGKT DSSYEKEKLN ERLAKLSGGV AVIKVGGASD VEVGEKKDRV TDALNATRAA
     VSEGIVPGGG AALLYASSAL AELAADPTLT EDQKTGVRIV MSAIKLPAIT IVKNAGGEGA
     VVIHQLLAEK KMQQGYDAQQ GKYVNMFEAG IIDPAKVVKT ALVDAASVAG LMITTEAAIT
     DIPAPAPAAG GGMDGMGGMG GMGGMGGMY