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Database: UniProt
Entry: A0A0A1TGH0_9HYPO
LinkDB: A0A0A1TGH0_9HYPO
Original site: A0A0A1TGH0_9HYPO 
ID   A0A0A1TGH0_9HYPO        Unreviewed;       483 AA.
AC   A0A0A1TGH0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|ARBA:ARBA00031396};
GN   ORFNames=VHEMI05208 {ECO:0000313|EMBL:CEJ89363.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ89363.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ89363.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000002; CEJ89363.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1TGH0; -.
DR   STRING; 1531966.A0A0A1TGH0; -.
DR   HOGENOM; CLU_033261_0_0_1; -.
DR   OrthoDB; 1329460at2759; -.
DR   Proteomes; UP000039046; 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:UP000039046}.
FT   DOMAIN          2..194
FT                   /note="Cdc37 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01071"
FT   DOMAIN          197..367
FT                   /note="Cdc37 Hsp90 binding"
FT                   /evidence="ECO:0000259|SMART:SM01070"
FT   DOMAIN          382..482
FT                   /note="Cdc37 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01069"
FT   REGION          176..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  53078 MW;  8A58E65E7A914DB7 CRC64;
     MPVDYSKWDA LELSDDSDVE VHPNVDKRSF IRAKQNQIHQ ERQQRKTKIE ALKYELVLHE
     GLRKRVSALL SSLKARADQA ATKNPAEVAF AAVMESAGQQ TDDKLPPLPE GLHTDPNQPK
     TYSAMLAGML DQVNKALDEK KPDDRYSSMV AEVESHEGQI NTLLKDSAAE LQKLEQEDKR
     KITSDSIHTG FDSSHVNKTT SSAESTKVEL LNPSFDTSGG SSSKKSQSAG GAASAADDDD
     EDAEASPAGI KFSQIASNNY SASLDFLSKN PQILTEKETD GLLVLAFDAA LERKDDLCRQ
     CVHQALLLQY CRALGKDGVA LFFKRVTTQG HQAQDLFIRD VQDTYMRIKN RAAEIVAERA
     NEPEGVEQIQ LHAVEPGTVI NISIPPADSE DTEIKRAREI FEGFAPEMKA ALETGELDKV
     NKVLGEMSVE DAEELVNLFS EANILSMEEQ IIDATTEQGK QQLKEIERAA AAAEDEGPTP
     DPE
//
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