ID   HSP90_BRUPA             Reviewed;         717 AA.
AC   O61998; O76825;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Heat shock protein 90;
GN   Name=HSP90;
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Cockroft A.C., Thompson F.J., Devaney E.;
RT   "Studies on hsp90 from the filarial nematode, Brugia pahangi.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC       maintenance and proper regulation of specific target proteins involved
CC       for instance in cell cycle control and signal transduction. Undergoes a
CC       functional cycle that is linked to its ATPase activity. This cycle
CC       probably induces conformational changes in the client proteins, thereby
CC       causing their activation. Interacts dynamically with various co-
CC       chaperones that modulate its substrate recognition, ATPase cycle and
CC       chaperone function (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC       repeat-containing proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; AJ005784; CAA06694.1; -; mRNA.
DR   EMBL; AJ005785; CAA06695.1; -; Genomic_DNA.
DR   AlphaFoldDB; O61998; -.
DR   SMR; O61998; -.
DR   STRING; 6280.O61998; -.
DR   Proteomes; UP000038020; Genome Assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..717
FT                   /note="Heat shock protein 90"
FT                   /id="PRO_0000062937"
FT   REGION          215..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           713..717
FT                   /note="TPR repeat-binding"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         382
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        126
FT                   /note="V -> A (in Ref. 1; CAA06694)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   717 AA;  82605 MW;  77F7D3D4F3A0A9DA CRC64;
     MSEEMNGETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR YQALTEPAEL
     ETGKELYIKI TPNKADKTLT IMDTGIGMTK ADLVNNLGTI AKSGTKAFME ALQAGADISM
     IGQFGVGFYS AFLVADKVVV ASKHNDDDCY QWESSAGGSF IIRQVNDPEL TRGTKITLYI
     KEDQTDYLEE RRIKEIVKKH SQFIGYPIKL TVEKERDKEV SDDEAEEEKK DEDKEKKEGE
     IEDVGEDEEE DKKDKDKKKK KIKEKYHEDE ELNKTKPIWT RNPDDISNEE YAEFYKSLSN
     DWEDHLAVKH FSVEGQLEFR ALLFVPQRAP FDLFENKKTK NAIKLYVRRV FIMENCDELM
     PEYLNFIKGV VDSEDLPLNI SREMLQQSKI LKVIRKNLVK KCLELFDEIA EDKDNFKKFY
     EQFSKNIKLG IHEDSTNRKK LSEFLRFYTS ASSEEMTSLK DYVSRMKENQ KQIYFITGES
     REAVASSAFV ERVKRRGFEV IYMTDPIDEY CVQQLKEYDG KKLVSVTKEG LELPESEEEK
     KKFEEDKVKF ENLCKVMKDI LEKKVEKVAV SNRLVSSPCC IVTSEYGWSA NMERIMKAQA
     LRDSSTMGYM AAKKHLEINP DHSVIKALRE RVEADKNDKT VKDLVVLLFE TALLSSGFSL
     EDPQLHASRI YRMIKLGLDI TEDEEEEAIA SVSGEKDECV PNLVGAEEDA SRMEEVD