ID   A0A1B0VC07_CLAPU        Unreviewed;       185 AA.
AC   A0A1B0VC07;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JUL-2024, entry version 17.
DE   SubName: Full=60 kDa chaperonin {ECO:0000313|EMBL:AMQ10014.1};
DE   Flags: Fragment;
GN   Name=cpn60 {ECO:0000313|EMBL:AMQ10014.1};
OS   Claviceps purpurea (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=5111 {ECO:0000313|EMBL:AMQ10014.1};
RN   [1] {ECO:0000313|EMBL:AMQ10014.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Dumonceaux T.J., Grafenhan T., Comte A.O., Links M.G., Hemmingsen S.M.;
RT   "Molecular grading for ergot on cereal grains reveals the burden of
RT   Claviceps purpurea DNA on crop seeds.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000256|ARBA:ARBA00006607}.
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DR   EMBL; KU145550; AMQ10014.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B0VC07; -.
DR   VEuPathDB; FungiDB:CPUR_01730; -.
DR   GO; GO:1990220; C:GroEL-GroES complex; IEA:TreeGrafter.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:TreeGrafter.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:TreeGrafter.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:TreeGrafter.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:TreeGrafter.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:TreeGrafter.
DR   GO; GO:0034514; P:mitochondrial unfolded protein response; IEA:TreeGrafter.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:TreeGrafter.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:TreeGrafter.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; IEA:TreeGrafter.
DR   GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IEA:TreeGrafter.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:TreeGrafter.
DR   Gene3D; 3.50.7.10; GroEL; 1.
DR   Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR   Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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   PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR   SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AMQ10014.1"
FT   NON_TER         185
FT                   /evidence="ECO:0000313|EMBL:AMQ10014.1"
SQ   SEQUENCE   185 AA;  20084 MW;  9F178B7262EB9AC2 CRC64;
     ATVLARAIFS ETVKNVAAGC NPMDLRRGIQ AAVDAVVKYL HEQKRDITTS SEIAQVATIS
     ANGDVHVGEM IANAMEKVGK EGVITVKEGK TMSDELEVTE GMRFDRGFVS PYFITDAKAQ
     KVEFENPLIL LSQKKISAVQ DIIPALEIST QTRRPLFIIA EDIDGEALAV CILNKLRGQL
     QVAAV
//