CH60_LEIMA
ID CH60_LEIMA Reviewed; 589 AA.
AC Q94596;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chaperonin HSP60, mitochondrial;
DE Short=Protein Cpn60;
DE AltName: Full=Heat shock protein 60;
DE AltName: Full=groEL protein;
DE Flags: Precursor;
GN Name=HSP60;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=9085922; DOI=10.1006/expr.1996.4137;
RA Rey-Ladino J.A., Joshi P.B., Singh B., Gupta R., Reiner N.E.;
RT "Leishmania major: molecular cloning, sequencing, and expression of the
RT heat shock protein 60 gene reveals unique carboxy terminal peptide
RT sequences.";
RL Exp. Parasitol. 85:249-263(1997).
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- INDUCTION: By heat shock. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; U59320; AAC13945.1; -; Genomic_DNA.
DR AlphaFoldDB; Q94596; -.
DR SMR; Q94596; -.
DR STRING; 5664.LmjF.32.1850; -.
DR VEuPathDB; TriTrypDB:LmjF.32.1850; -.
DR VEuPathDB; TriTrypDB:LMJLV39_320024800; -.
DR VEuPathDB; TriTrypDB:LMJSD75_320024800; -.
DR eggNOG; KOG0356; Eukaryota.
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 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding; Stress response;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..589
FT /note="Chaperonin HSP60, mitochondrial"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005035"
FT REGION 550..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 63523 MW; 14021344FAAC3573 CRC64;
MLSRTVPRCV KYGSTPKDIR YGMEARNALL AGVENLVKAV GVTLGPKGRN VILEMPYACP
KITKDGVTVA KSIEFEDSFE NLGANLVRQV AGLTNDNAGD GTTTATVLSG AIFKEGFRSV
ASGTNPMDLK RGIDLACREV LISLAEQSRP VTSKSEITQV AMISANMDQE IGSLIGDAMQ
QVGKDGVITT QEGRSLNTEL ELVEGMSFER GYTSPYFVTN TKAQRCELEN ALVYVANRKL
TSVAHILPAL NYAIQQKRPL LVIAEDVEGE AMHTFLYNKI QGRISGCAVK APGFGDMRIN
QLQDIAVFTG SQMISEDLGL SLDQNDFSER FLGTCRKVTV SRDECILMEG GGSAIAVEER
VQMIKDMISA EDHEYNRERL VERLAKLSGG VAVIKVGGAS EVEINEKKDR IIDALNATRA
AVSEGILAGG GTGLLMASLR LESISKDRRL PPDIRTGVNI VKKAIGLPAR YIANNAGVEG
SVVAGKVLAR KDPSFGYNAQ TGEYVNMFEA GIIDPMKVVK SAVVNACSVA GMMITTEAAV
VEKDLLGREK RIEDEGMEDK EKKRSVDKLR KQVNEAGRTD AQDGAADEV
