ID   CH61_CUCMA              Reviewed;         575 AA.
AC   Q05045;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chaperonin CPN60-1, mitochondrial;
DE   AltName: Full=HSP60-1;
DE   Flags: Precursor;
GN   Name=CPN60-1;
OS   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Cotyledon;
RX   PubMed=1356771; DOI=10.1111/j.1432-1033.1992.tb17309.x;
RA   Tsugeki R., Mori H., Nishimura M.;
RT   "Purification, cDNA cloning and Northern-blot analysis of mitochondrial
RT   chaperonin 60 from pumpkin cotyledons.";
RL   Eur. J. Biochem. 209:453-458(1992).
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   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; X70867; CAA50217.1; -; mRNA.
DR   AlphaFoldDB; Q05045; -.
DR   SMR; Q05045; -.
DR   PRIDE; Q05045; -.
DR   OrthoDB; 415781at2759; -.
DR   Proteomes; UP000504608; Unplaced.
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; 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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Stress response; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT   CHAIN           33..575
FT                   /note="Chaperonin CPN60-1, mitochondrial"
FT                   /id="PRO_0000005011"
SQ   SEQUENCE   575 AA;  61055 MW;  D4646FE516B1DFBB CRC64;
     MHRFATGLAS KARLARNGAN QIASRSNWRR NYAAKDVKFG VEARGLMLKG VEDLADAVKV
     TMGPKGRTVV IEQSFGAPKV TKDGVTVAKS IEFKDKVKNV GASLVKQVAN ATNDVAGDGT
     TCATILTKAI FTEGCKSVAS GMNAMDLRRG ISMAVDSVVT NLKSRARMIS TSEEIAQVGT
     ISANGEREIG ELIAKAMEKV GKEGVITISD GKTMDNELEV VEGMKLDRGY ISPYFITNQK
     NQKCELDDPL IIIYEKKISS INAVVKVLEL ALKKQRPLLI VSEDVESEAL ATLILNKLRA
     GIKVCAIKAP GFGENRKAGL QDLAVLTGGQ VITEELGMNL EKVDLDMLGS CKKITISKDD
     TVILDGAGDK KAIEERCDQI RSGIEASTSD YDKEKLQERL AKLSGGVAVL KIGGASEAEV
     GEKKDRVTDA LNATKAAVEE GIVPGGGVAL LYASKELDKL PTANFDQKIG VQIIQNALKT
     PVHTIASNAG VEGAVVVGKL LEQDDPDLGY DAAKGEYVDM VKAGIIDPLK VIRTALVDAA
     SVSSLMTTTE VVVVELPKDE NEVPAMGGGM GGMDY