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
//