ID A0A0W0G108_9AGAR Unreviewed; 486 AA.
AC A0A0W0G108;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN ORFNames=WG66_5202 {ECO:0000313|EMBL:KTB42256.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB42256.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB42256.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB42256.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the CDC37 family.
CC {ECO:0000256|ARBA:ARBA00006222}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTB42256.1}.
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DR EMBL; LATX01001365; KTB42256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0G108; -.
DR eggNOG; KOG2260; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
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:SF4; HSP90 CO-CHAPERONE CDC37; 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.
DR SUPFAM; SSF101391; Hsp90 co-chaperone CDC37; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT DOMAIN 2..195
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 209..371
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 386..485
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 224..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 158..187
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 486 AA; 54583 MW; F0262E2B936479B6 CRC64;
MPLNYSKWDQ LELSDDSDIE GHPNVDKKSL IRWKQRDIHE KREARKDKIA SLRAQIDCNT
VLLPRIREIR TNLTTPASIP PTTYFNNLVE QLEKNPSKDC PPGNDPSKLE HTYDGMILNL
LQLVSQQAKE KIKDASVLDN EKDEKLAQGL IDGMEFHCEE LKKTIDRDQA ELEAEEKEQK
KHITSDDLHE GFSSKYVPAK LAPPAVPVSK IEKPKSKQTV TEYEVLNPTP GPDSVLPESS
VLTEDDDSLP ELTPSLQAFA KLPLWAYEKS FEFIQAHRDV VVPGAADALL VAAFNAQTDG
KGRYAKQCIH QSLLLQYCEK LGPDGVQVFF RKMISGDKRA EKVFVDDVEN TYGHLVNRVQ
KSKEEIMGGK EQIQLVPESA DQQITFNVPS GPPPENIILE GPGTENMDIE EVRKALQYRW
EVFQGFPQAL QTALTENSLQ KVNEVLANMD VTEAESIVGR LDMAGILSFA EGGIRDETGR
AEKKEK
//
