HSP60_CANAL
ID HSP60_CANAL Reviewed; 566 AA.
AC O74261; A0A1D8PT81; Q59U15;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Heat shock protein 60, mitochondrial;
DE AltName: Full=60 kDa chaperonin;
DE AltName: Full=Protein Cpn60;
DE Flags: Precursor;
GN Name=HSP60; OrderedLocusNames=CAALFM_CR06490CA;
GN ORFNames=CaO19.717, CaO19.8336;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061;
RA Swoboda R.K., Gow N.A.R., Fidel P.L. Jr., Brown A.J.P.;
RT "Isolation and characterization of the HSP60 gene from the pathogenic
RT fungus Candida albicans.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: May participate in assembly and/or disassembly of proteins
CC imported into the mitochondrion. HSP60 are ATPases and have affinity
CC for unfolded proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; AF085694; AAC34885.1; -; Genomic_DNA.
DR EMBL; CP017630; AOW31348.1; -; Genomic_DNA.
DR RefSeq; XP_713077.1; XM_707984.2.
DR AlphaFoldDB; O74261; -.
DR SMR; O74261; -.
DR BioGRID; 1228332; 2.
DR STRING; 237561.O74261; -.
DR COMPLUYEAST-2DPAGE; O74261; -.
DR PRIDE; O74261; -.
DR GeneID; 3645275; -.
DR KEGG; cal:CAALFM_CR06490CA; -.
DR CGD; CAL0000174464; HSP60.
DR VEuPathDB; FungiDB:CR_06490C_A; -.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; O74261; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 415781at2759; -.
DR PRO; PR:O74261; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0006458; P:'de novo' protein folding; IEA:EnsemblFungi.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:EnsemblFungi.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..566
FT /note="Heat shock protein 60, mitochondrial"
FT /id="PRO_0000005041"
FT REGION 546..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 60126 MW; FAD9C690FE3EB15C CRC64;
MLRVNSKSSI KTFVRHLSHK ELKFGVEGRA ALLKGVNTLA DAVSVTLGPK GRNVLIEQQF
GAPKITKDGV TVAKAITLED KFEDLGAKLL QEVASKTNES AGDGTTSATV LGRSIFTESV
KNVAAGCNPM DLRRGSQAAV EAVIEFLQKN KKEITTSEEI AQVATISANG DKHIGDLLAN
AMEKVGKEGV ITVKEGKTLE DELEVTEGMK FDRGFISPYF ITNTKTGKVE FENPLILLSE
KKISSIQDIL PSLELSNQTR RPLLIIAEDV DGEALAACIL NKLRGQVQVC AVKAPGFGDN
RKNTLGDIAI LSGGTVFTEE LDIKPENATI EQLGSAGAVT ITKEDTVLLN GEGSKDNLEA
RCEQIRSVIA DVHTTEYEKE KLQERLAKLS GGVAVIKVGG ASEVEVGEKK DRYEDALNAT
RAAVEEGILP GGGTALIKAT KILDEVKEKA VNFDQKLGVD TIRAAITKPA KRIIENAGEE
GAVIVGKIYD EPEFNKGYDS QKGEFTDMIA AGIIDPFKVV KNGLVDASGV ASLLATTECA
IVDAPQPKGS PAAPPAPGMG GMPGMF
