ID A0A0D2BCI2_9EURO Unreviewed; 518 AA.
AC A0A0D2BCI2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN ORFNames=PV05_11486 {ECO:0000313|EMBL:KIW49841.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW49841.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW49841.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW49841.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-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}.
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DR EMBL; KN847323; KIW49841.1; -; Genomic_DNA.
DR RefSeq; XP_013310425.1; XM_013454971.1.
DR AlphaFoldDB; A0A0D2BCI2; -.
DR STRING; 348802.A0A0D2BCI2; -.
DR GeneID; 25333394; -.
DR HOGENOM; CLU_033261_0_0_1; -.
DR OrthoDB; 1329460at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 2..195
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 198..389
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 408..507
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 97..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 58093 MW; 4B61F43C3AEE9FF5 CRC64;
MPISYDKWDR LEVSDDSDVE VHPNVDTKSF IRAKQRQIHE QRAQRKHEIE TLKYERIIND
GLLERINALL DALKKHQEDA ATKNPDELVF QSLIESAGDP AKDEPPKPPE GVYTHQKEPQ
PRYSKMMGAL VDQVKKEVDE KNSPDRYKDF VEGVNGHLTK VQKLQQDLLT RLAQLEKEAT
AKITSEDLHE GFSYSSVNKP KHASAKSEKP REPAKTETVE LLNAPKGLSS KTRDALKSPD
EAVSSGAEAD VEDDALTNKH EDEEDEASLK LTPAGKQFAK IKLGDYRTCL QFISEHPEIV
NEHTQDALMI EAFNAQMKGQ DTYAKGCVHQ SLLIQYCRQL GRDGVGLFFK RITTKGHQAQ
QVFSKDLAET YERIKTRAAE LSKEEGTDPA GVEQIQLHAV EPGTEIHINV PQAGSEDPIE
QQSREIFERF PPGLQRALES GSLDEVNVVL GKMSVDEAEE IVELLGQGGM LSLQEGVIDA
TNEEGQKRLQ EIEEEERRKK AEKGQPIQED EPGEAVEA
//
