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Database: UniProt
Entry: A0A168HQU5_CORDF
LinkDB: A0A168HQU5_CORDF
Original site: A0A168HQU5_CORDF 
ID   A0A168HQU5_CORDF        Unreviewed;       488 AA.
AC   A0A168HQU5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN   ORFNames=LEL_04938 {ECO:0000313|EMBL:OAA78115.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA78115.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA78115.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA78115.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA78115.1}.
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DR   EMBL; AZHF01000003; OAA78115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168HQU5; -.
DR   STRING; 1081108.A0A168HQU5; -.
DR   OrthoDB; 1329460at2759; -.
DR   Proteomes; UP000076881; 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:UP000076881}.
FT   DOMAIN          2..195
FT                   /note="Cdc37 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01071"
FT   DOMAIN          198..366
FT                   /note="Cdc37 Hsp90 binding"
FT                   /evidence="ECO:0000259|SMART:SM01070"
FT   DOMAIN          383..482
FT                   /note="Cdc37 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01069"
FT   REGION          186..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  53816 MW;  AF00F7DCCE537ED5 CRC64;
     MPVDYSKWDA LELSDDSDVE VHPNVDKKSF IRAKQTQIHQ ERQQRKHRME ALKYEVALHQ
     ALLKRISALV AALRSRASEA AATENPGQLA FQAVMESAGD QKDDDLPPVP EGLRVDPNQP
     KTYSAMMAGL LDQVNKAMEA KQPDDRYTAM LEEIGVHETQ VRTLIKESSD ELAKLEKEEG
     KKITSEGIHT GFDSSFVSKA TGTGGDTTQV ELLNPNHKPG ESSSSASKEG SSSKDSKDDD
     DMEASPAARK FADIRPNDYS ASLDHLVKHP QILTEKETDG LLVLAFDAAL ESKDERSKQC
     VHQALLLQYC RSLGRDGVGL FFKRITASGG NNAKEVFYKD VHDTYLRIRT RAREIVAERA
     KEPAEGVEQI QLHAVEPGTV ISISVPAADS EDPEVQEARE IYEHFSEEMR TALETGELDK
     VNEVLGNMSV EEAEEYVNLF GEANILSLEE QIIDGTTDEG KQQIKDLEAK AAAERAAEAD
     EGPTGDPE
//
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