ID A0A395HAV8_9EURO Unreviewed; 491 AA.
AC A0A395HAV8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN ORFNames=BO80DRAFT_400281 {ECO:0000313|EMBL:RAL04068.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL04068.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL04068.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL04068.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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; KZ824425; RAL04068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HAV8; -.
DR STRING; 1448316.A0A395HAV8; -.
DR VEuPathDB; FungiDB:BO80DRAFT_400281; -.
DR OrthoDB; 1329460at2759; -.
DR Proteomes; UP000249402; 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:UP000249402}.
FT DOMAIN 2..191
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 199..365
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 382..479
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 95..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 54710 MW; 23A862EB8650F4CC CRC64;
MVLDYSKWDA LELSDDSDIE VHPNVDKRSF IRAKQAQIHQ QRSQRRYEID TLKYEHIVND
GLLSRIDKLL TSLKQNEGSK SVEEVIFQNL MEFAGNPSED HPPAPPAGVH TQEKEQPKYS
QMMSALLDQV KKEMGDASTE DLYQEYIKGV KRHEDKVQGL QMELLQRLAQ LEKEERSKIT
SDKLHEGFNT SHIAKGGDAK GTGSSQQTGT VELLNPGAST AGSSQLAAAD DDDEEEDPED
IKASDLAKRF AKIDRSDYRA LLQFVSANPQ IVAEKETDGL LVEAFNSQME GKEDYARTCV
HQGLLLQYCR SLGRDGISLF FKRITTADHQ AGTLFRNDVN ETYNKIKTRA AELARDSSAS
NDPAGVEQIQ LHAVDPNTKI TINIPAAESN EPIEIEARKV FESFSKDMQA ALASESLDEV
NKVLGELSVE EAEDVVEKLG QSGMLSLEEG IVDATTEEGR KKLEEIEAEN KREREEKQEI
GEPGGDVTEL D
//
