ID   A0A3B4UMR1_SERDU        Unreviewed;       355 AA.
AC   A0A3B4UMR1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Hsp90 co-chaperone Cdc37 {ECO:0000256|ARBA:ARBA00020496, ECO:0000256|RuleBase:RU369110};
DE   AltName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|RuleBase:RU369110};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000019622.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000019622.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|RuleBase:RU369110}.
CC   -!- SUBUNIT: Forms a complex with Hsp90. {ECO:0000256|RuleBase:RU369110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU369110}.
CC   -!- SIMILARITY: Belongs to the CDC37 family.
CC       {ECO:0000256|ARBA:ARBA00006222, ECO:0000256|RuleBase:RU369110}.
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DR   AlphaFoldDB; A0A3B4UMR1; -.
DR   Ensembl; ENSSDUT00000019971.1; ENSSDUP00000019622.1; ENSSDUG00000014231.1.
DR   GeneTree; ENSGT00390000013443; -.
DR   OMA; IVMKFIL; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR   Gene3D; 6.10.140.250; -; 1.
DR   Gene3D; 1.20.58.610; Cdc37, Hsp90 binding domain; 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; CDC37-RELATED; 1.
DR   PANTHER; PTHR12800:SF3; HSP90 CO-CHAPERONE CDC37; 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.
DR   SUPFAM; SSF101391; Hsp90 co-chaperone CDC37; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|RuleBase:RU369110};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU369110}.
FT   DOMAIN          6..139
FT                   /note="Cdc37 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01071"
FT   DOMAIN          132..292
FT                   /note="Cdc37 Hsp90 binding"
FT                   /evidence="ECO:0000259|SMART:SM01070"
FT   DOMAIN          296..354
FT                   /note="Cdc37 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01069"
FT   COILED          45..123
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   355 AA;  41820 MW;  707C292502FC7610 CRC64;
     MSTRAGVDYS AWDHIYVSDD EDVASPYVDT PSLFRMRHRA RLERMAEFQQ KGEDLENNFA
     ECKRLLEEAQ GRLRELQQVK KEGEEDEEQE AELKKVQTEV RELKKDQKAF EKMMEQHRRE
     EKKLPWNVDT ISKEGFSKSV LNIQPVTKEE TEEVVEKHKT FVQKYTKEIK HFGMLRRWDD
     SQKYLSDNPH LVCEETANYL VVICIDFEID EKHALMEQVA HQAIVMQFIL DLARTLKVDP
     RGCFRQFFSK IKTADKPYQD AFDRELELLK ERVRSCAQIR MEDAMKEVEE EERQKRLGPG
     GLDPVEVYES LPKVTTNTHM HTLEGKYHLR RCIDSGLWVP DSGQGNDEEE EEEEG
//