ID   CH63_HELVI              Reviewed;         569 AA.
AC   P25420;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=63 kDa chaperonin, mitochondrial;
DE   AltName: Full=p63;
DE   Flags: Precursor;
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-53.
RC   TISSUE=Testis;
RX   PubMed=1974308; DOI=10.1016/0022-2836(90)90190-w;
RA   Miller S.G., Leclerc R.F., Erdos G.W.;
RT   "Identification and characterization of a testis-specific isoform of a
RT   chaperonin in a moth, Heliothis virescens.";
RL   J. Mol. Biol. 214:407-422(1990).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a single seven-member ring complex, in tight association
CC       with the p60 protein.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- DEVELOPMENTAL STAGE: From the latter half of the larval final-instar,
CC       through the first two days of pupal development.
CC   -!- MISCELLANEOUS: Shows ATPase activity.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; X56034; CAA39509.1; -; Genomic_DNA.
DR   PIR; S11035; S11035.
DR   AlphaFoldDB; P25420; -.
DR   SMR; P25420; -.
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   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; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1974308"
FT   CHAIN           30..569
FT                   /note="63 kDa chaperonin, mitochondrial"
FT                   /id="PRO_0000005034"
SQ   SEQUENCE   569 AA;  61508 MW;  1089DB9E87BA3CCA CRC64;
     MFKMYRSPHI TRNSFKYLKA TNINSCRFYA KEVRFGPDVR SLMLQGVDIL ADADDVTMGP
     KGVNVILAKN LGPPKITKDG VTVAKGIDLK DKFQNIGARL VQNVANKTNE EAGDGTTTAT
     VLARPIAKEG FENISRGANP IEIRKGVMLA VESVKRQLKE MSKPVNTSEE IEQVATISAN
     GDESIGKLIA AAMNRVGKNG VITVKDGKTL EDELEIIEGM KFDRGYVSPY FINSNKGPKV
     EYNDALVLYS EKKIYYASQV VPALELANSQ KKPLVIIAED YDGEPLSVLV VNKLKIGLPV
     VAVKAPGFGE YRTNALLDMA AATGGVFEDD TNLVRLEDCQ AESFGQVGEV IITKDSTLLL
     KGKGDPNEIK QRIDQIKEEL ETATSNYDRE RLIDRLGRLQ SGVAVLLIGG CSEVEVNEKK
     DRVNDALNAT RAAVEEGIVP GGGAALLRCI PALDLLKPAN KDQEIGVSII KKALRTPCIT
     IASNAGFDGA VVVSKVEDMG PEYGYDALNN EYVNMIEKGI IDPTKVVRRA LTDASGVASL
     LTTAEAVICD MPKQKDPPPE YAPIGGGDY