ID   CH61_MAIZE              Reviewed;         577 AA.
AC   P29185; Q43251; Q43252;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Chaperonin CPN60-1, mitochondrial;
DE   AltName: Full=HSP60-1;
DE   Flags: Precursor;
GN   Name=CPN60I; Synonyms=CPNA;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 35-70.
RC   STRAIN=cv. Black Mexican Sweet; TISSUE=Seed;
RX   PubMed=1349837; DOI=10.1007/bf00019202;
RA   Prasad T.K., Stewart C.R.;
RT   "cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial
RT   chaperonin HSP60 and gene expression during seed germination and heat
RT   shock.";
RL   Plant Mol. Biol. 18:873-885(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. B73;
RA   Close P.S.;
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. MUTIND-FR7205024;
RA   Burt W.J.;
RL   Submitted (OCT-1992) 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   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; Z11546; CAA77645.1; -; mRNA.
DR   EMBL; L21007; AAA33450.1; -; Genomic_DNA.
DR   EMBL; Z12114; CAA78100.1; -; mRNA.
DR   PIR; S20875; S20875.
DR   PIR; S26582; S26582.
DR   RefSeq; NP_001105716.1; NM_001112246.1.
DR   AlphaFoldDB; P29185; -.
DR   SMR; P29185; -.
DR   PRIDE; P29185; -.
DR   EnsemblPlants; Zm00001eb222300_T002; Zm00001eb222300_P002; Zm00001eb222300.
DR   GeneID; 542736; -.
DR   Gramene; Zm00001eb222300_T002; Zm00001eb222300_P002; Zm00001eb222300.
DR   KEGG; zma:542736; -.
DR   MaizeGDB; 65669; -.
DR   OMA; TDTDKME; -.
DR   OrthoDB; 415781at2759; -.
DR   Proteomes; UP000007305; Chromosome 5.
DR   ExpressionAtlas; P29185; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:AgBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0051117; F:ATPase binding; IPI:AgBase.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1349837"
FT   CHAIN           35..577
FT                   /note="Chaperonin CPN60-1, mitochondrial"
FT                   /id="PRO_0000005014"
FT   CONFLICT        21
FT                   /note="T -> A (in Ref. 3; CAA78100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108..109
FT                   /note="KQ -> NR (in Ref. 1; CAA77645)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="A -> D (in Ref. 1; CAA77645)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="D -> N (in Ref. 1; CAA77645)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="S -> P (in Ref. 3; CAA78100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328
FT                   /note="L -> F (in Ref. 1; CAA77645)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="I -> L (in Ref. 1; CAA77645)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        403
FT                   /note="A -> P (in Ref. 2; AAA33450)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   577 AA;  61211 MW;  31D3BFFD46701C0B CRC64;
     MYRAAASLAS KARQAGNSLA TRQVGSRLAW SRNYAAKDIK FGVEARALML RGVEELADAV
     KVTMGPKGRN VVIEQSFGAP KVTKDGVTVA KSIEFKDRVK NVGASLVKQV ANATNDTAGD
     GTTCATVLTK AIFTEGCKSV AAGMNAMDLR RGISMAVDAV VTNLKGMARM ISTSEEIAQV
     GTISANGERE IGELIAKAME KVGKEGVITI ADGNTLYNEL EVVEGMKLDR GYISPYFITN
     SKTQKCELED PLILIHDKKV TNMHAVVKVL EMALKKQKPL LIVAEDVESE ALGTLIINKL
     RAGIKVCAVK APGFGENRKA NLQDLAILTG GEVITEELGM NLENFEPHML GTCKKVTVSK
     DDTVILDGAG DKKSIEERAE QIRSAIENST SDYDKEKLQE RLAKLSGGVA VLKIGGASEA
     EVGEKKDRVT DALNATKAAV EEGIVPGGGV ALLYASKELD KLQTANFDQK IGVQIIQNAL
     KTPVHTIASN AGVEGAVVVG KLLEQENTDL GYDAAKGEYV DMVKTGIIDP LKVIRTALVD
     AASVSSLMTT TESIIVEIPK EEAPAPAMGG GMGGMDY