ID   CH60_PLAFG              Reviewed;         700 AA.
AC   P34940;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Chaperonin CPN60, mitochondrial;
DE   Flags: Precursor;
OS   Plasmodium falciparum (isolate FCR-3 / Gambia).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5838;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7915821; DOI=10.1016/0166-6851(94)90131-7;
RA   Holloway S.P., Min W., Inselburg J.I.;
RT   "Isolation and characterization of a chaperonin-60 gene of the human
RT   malaria parasite Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 64:25-32(1994).
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 matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; X75420; CAA53172.1; -; Genomic_DNA.
DR   PIR; S38426; S38426.
DR   AlphaFoldDB; P34940; -.
DR   SMR; P34940; -.
DR   PRIDE; P34940; -.
DR   GO; GO:0005759; C:mitochondrial matrix; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding; Stress response;
KW   Transit peptide.
FT   TRANSIT         1..9
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           10..700
FT                   /note="Chaperonin CPN60, mitochondrial"
FT                   /id="PRO_0000005037"
FT   REGION          636..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..700
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  79445 MW;  AE1DB362B666D382 CRC64;
     MRMKRIHILF VVIFLLCLRY GYSIKKKRSP NNKNRLFINK RLKYINSKII SRRKENYVKM
     KMTENKVKGK DIIYGNECRN ELLKGILTVS DVVKLTLGPR GRNVLLEKEY GSPLIINDGV
     TIAKNISLKD RKKNNGVKLM QESTNISNDK AGDGTSSTAL MTATITKKGI EQVNRNHNPI
     PIQRGIQLAS KMIIEKIKSL STPIKTYKDI LNIATIASNN DVHMGQIIAN AYDKLGKNAA
     IILDDNADIN DKLEFTEGYN FDRGIINPYL LYNENKDYIE YSNVSTLITD QNIDNIQSIL
     PILEIFAKNK QPLCIIADDF SNEVLQTLII NKLKGAIKVL CIVTNSKYIS ADVGLDLNNL
     HNNMSSFDNN YLSLLGSANT LIVKKDRTSL ITKEEYKKEI DERINVLKKE YEETTSKYDK
     EKLNERIAAL SGGIAKILIG GNSETEQKER KFKYEDATNA VKSAIDIGYV PGGGVTYLEI
     IKSNFIQEIH KKIEEDLQIS SNNDEKKYLE LIGNLESEME LQKMGANIVV SSLDVITKQI
     ADNAGVNGDN VVKIILNSKD KYGFGYDVNT NKFVNMVEKG IIDSTNVIIS VIKNSCSIAS
     MVLTTECMMV DHEKKDKGIL DSSINSPNYL SKHRRTYKHK LHDDEDTDED DEEDEDDEDD
     EDDLDDDDYD DEDEEDEEDE EDEDDEDDED SMNDEYNYDE