ID   TCM62_YEAS7             Reviewed;         572 AA.
AC   A6ZKY8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Mitochondrial chaperone TCM62;
DE   Flags: Precursor;
GN   Name=TCM62; ORFNames=SCY_0258;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Chaperone. Required for the assembly of succinate
CC       dehydrogenase subunits. Ensures mitochondrial gene expression at
CC       elevated temperatures and prevents heat-aggregation of the ribosomal
CC       subunit VAR1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a high molecular mass protein complex of approximately
CC       850 kDa. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; AAFW02000011; EDN64657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZKY8; -.
DR   SMR; A6ZKY8; -.
DR   PRIDE; A6ZKY8; -.
DR   EnsemblFungi; EDN64657; EDN64657; SCY_0258.
DR   HOGENOM; CLU_485763_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 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   SUPFAM; SSF52029; SSF52029; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Stress response;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..572
FT                   /note="Mitochondrial chaperone TCM62"
FT                   /id="PRO_0000377650"
FT   TOPO_DOM        17..471
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        489..572
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   572 AA;  64266 MW;  7C9FE642B3DBD264 CRC64;
     MLRNCLRKLG NHQTKCSVKT LHTPIYRTKN LQVLRDTLSG IKLLEKIITS SSYNKTLIYE
     PKYKSKPQVV SSHDTMRLHN VMRELLDSLQ VDEATNTRLQ SNRPRKLGRV GLQLFMDCIQ
     DNLTATSTSL TCSLLEHYFK YPEKEVTNGI KAGLRYIRDF LAKNKIIVKS QNDVDALVEQ
     LTMSSSDSQS IKRVLKAINY ELFSDDIVRV INGNKTYDEV DVSKGWKYPA GILDSNEAYL
     RSLELPTKKL VSIDKDMLVL MYDGTLRDAN KILPTITYAR KLRKSILLIV NGDCTGDALT
     SVTINNNRNK RENNESRIVV LKYSKKANND LAPQENLDFI KFLRLPCGYD SIYSPEYSPL
     VPSKMCADKY YGSIESIKAT TGEAFLYNSI DAEAIPNKVP KSFLQNTVTL SIGGHNEIEI
     DRRRNAIDNC LNNVLCHGLA KGFIPGYGIS LLKAIPGLNE LKANEPNFMT KVGINAVLSA
     VILPSEVAFK NAYGYNYYEI NSLIAGAINE KSFPMAKFSP NSEPVNTVKD GNLEPWSKMD
     SCLAGVETFI ELLTSCNTII TCVYKKPERH KA