ID A0A3Q0GN29_ALLSI Unreviewed; 340 AA.
AC A0A3Q0GN29;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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};
GN Name=CDC37 {ECO:0000313|RefSeq:XP_025059588.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025059588.1};
RN [1] {ECO:0000313|RefSeq:XP_025059588.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_025059588.1; XM_025203803.1.
DR AlphaFoldDB; A0A3Q0GN29; -.
DR Proteomes; UP000189705; 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; PF08564; CDC37_C; 1.
DR Pfam; PF08565; CDC37_M; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT DOMAIN 1..93
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 86..247
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 251..339
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 313..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..74
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 318..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 39905 MW; 14C44619B187A1BB CRC64;
MERMEQFQKE KEELDKGCRE CKRKLAECQR KMMELQLAAP GGGQAELQRL QAEAQQLRSE
ERGWENKLEE LRKKEKNMPW NVDTLSKDGF SKSVFNIKTE EKDESEEQKE KKHKTFVQKY
EKQIKHFGML RRWDDSQKYL SDNPHLVCEE TANYLVIWCI DLEVEEKHAL MEQVAHQTIV
MQFILELAKS LKVDPRACFR QFFTKIKTAD QQYMEGFNDE LEAFKERVRG RAKVRIEKAM
KEYEEEERQK RLGPGGLDPV EVYESLPSEL QKCFDVKDVQ MLQDTISKMD PTEAKYHMQR
CIDSGLWVPN AKATEGAEKG SAEAEPVYEE LAKEGGEEEK
//
