ID   CDC37_TETFL             Reviewed;         377 AA.
AC   Q9DGQ7;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Hsp90 co-chaperone Cdc37;
DE   AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
DE   AltName: Full=p50Cdc37;
GN   Name=cdc37;
OS   Tetraodon fluviatilis (Green pufferfish) (Chelonodon fluviatilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=47145;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11072077; DOI=10.1016/s0167-4781(00)00138-x;
RA   Tsai S.C., Leu J.H., Chou C.M., Yeh M.S., Huang F.L., Huang C.J.;
RT   "Genomic organization and the promoter region of the round-spotted
RT   pufferfish (Tetraodon fluviatilis) CDC37 gene.";
RL   Biochim. Biophys. Acta 1494:144-148(2000).
CC   -!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
CC       their interaction with the Hsp90 complex, resulting in stabilization
CC       and promotion of their activity. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with Hsp90. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR   EMBL; AF091237; AAG00066.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9DGQ7; -.
DR   SMR; Q9DGQ7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR   Gene3D; 1.20.58.610; -; 1.
DR   InterPro; IPR004918; Cdc37.
DR   InterPro; IPR013873; Cdc37_C.
DR   InterPro; IPR013874; Cdc37_Hsp90-bd.
DR   InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR   InterPro; IPR013855; Cdc37_N_dom.
DR   PANTHER; PTHR12800; PTHR12800; 1.
DR   Pfam; PF08564; CDC37_C; 1.
DR   Pfam; PF08565; CDC37_M; 1.
DR   Pfam; PF03234; CDC37_N; 1.
DR   SMART; SM01069; CDC37_C; 1.
DR   SMART; SM01070; CDC37_M; 1.
DR   SMART; SM01071; CDC37_N; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm.
FT   CHAIN           1..377
FT                   /note="Hsp90 co-chaperone Cdc37"
FT                   /id="PRO_0000195061"
FT   REGION          339..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   377 AA;  44482 MW;  F8BD12F81F786A6D CRC64;
     MSRIDYSVWD HIEVSDDEDV SHPNIDTPSL FRWRHQARVE RMEDFKKKGD DLNKGLQECR
     RKLAEAQKKV RELSISAAGD AKAELTKTQT EEKKLKKEER DWARKLEEHN HEEKKMPWNV
     DTLSKDGFSK SIVNVKADSA EDTEEEKEKK HKTFVERYEK QIKHFGMLHR WDDSQRYLSD
     NPDLVCEETA NYLVIMCIDL EVEEKHALME QVAHQTIVMQ FILELAKSLK VDPRGCFRQF
     FEKIKTADQQ YQDAFNDELE SFKERVRGRA KIRIEKAMKE YEEEERQKRL GPGGLDPVEV
     YESLPPEMQK CFDEKDIQML QDVITKMDPT EAKAHMKRCI DSGLWVPNSK MDESDEKEDG
     STYEEVKQEQ EEPAKKE