ID   CDC37_CHICK             Reviewed;         393 AA.
AC   O57476;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Hsp90 co-chaperone Cdc37;
DE   AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
DE   AltName: Full=p50Cdc37;
GN   Name=CDC37;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9452487; DOI=10.1074/jbc.273.6.3598;
RA   Huang L., Grammatikakis N., Toole B.P.;
RT   "Organization of the chick CDC37 gene.";
RL   J. Biol. Chem. 273:3598-3603(1998).
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.
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; AF035530; AAB91998.1; -; mRNA.
DR   RefSeq; NP_990025.1; NM_204694.1.
DR   AlphaFoldDB; O57476; -.
DR   SMR; O57476; -.
DR   BioGRID; 675719; 1.
DR   GeneID; 395430; -.
DR   KEGG; gga:395430; -.
DR   CTD; 11140; -.
DR   VEuPathDB; HostDB:geneid_395430; -.
DR   InParanoid; O57476; -.
DR   OrthoDB; 786744at2759; -.
DR   PhylomeDB; O57476; -.
DR   PRO; PR:O57476; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..393
FT                   /note="Hsp90 co-chaperone Cdc37"
FT                   /id="PRO_0000195060"
FT   REGION          352..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   393 AA;  45608 MW;  12DC9A6DE8BE388A CRC64;
     MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DKGCRECKRK
     LAECQKKLKE LEVAEPGGGS GGGRGERERL QAEAQQLRHE ERNWESKMEE LRKKEKNMPW
     NVHTLSKDGF SKSVFNVKAE EKEETEEQKE QKHKTFVERH EKQIKHFGML RRWDDSQKYL
     SDNPHLVCEE TANYLVIWCI DLEVEEKQAL MEQVAHQTIV MQFILELAKS LKVDPRACFR
     QFFTKIKTAD QQYMEGFNDE LEAFKERVRG RAKARIERAM REYEEEERQK RLGPGGLDPV
     DVYESLPPEL QKCFDAKDVQ MLQDTISRMD PTEAKYHMQR CIDSGLWVPN AKAAAEGGGQ
     GGAHGQPGGA DSEALYEEIP KESGEEEGGE GKA