ID   HSP90_PODAS             Reviewed;         701 AA.
AC   O43109;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Heat shock protein 90 homolog;
DE   AltName: Full=Suppressor of vegetative incompatibility MOD-E;
GN   Name=MOD-E;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=9335595; DOI=10.1093/genetics/147.2.581;
RA   Loubradou G., Begueret J., Turcq B.;
RT   "A mutation in an HSP90 gene affects the sexual cycle and suppresses
RT   vegetative incompatibility in the fungus Podospora anserina.";
RL   Genetics 147:581-588(1997).
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; U81165; AAB97626.1; -; Genomic_DNA.
DR   AlphaFoldDB; O43109; -.
DR   SMR; O43109; -.
DR   PRIDE; O43109; -.
DR   VEuPathDB; FungiDB:PODANS_2_3760; -.
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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding.
FT   CHAIN           1..701
FT                   /note="Heat shock protein 90 homolog"
FT                   /id="PRO_0000062962"
FT   REGION          212..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           697..701
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        239..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         372
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   701 AA;  79323 MW;  E98A6A541406AACD CRC64;
     MAETFEFQAE ISQLLSLIIN TVYSNKEIFL RELVSNASDA LDKIRYESLS DPSKLDTGKD
     LRIDIIPDKE NKTLTIQDTG IGMTKADLVN NLGTIARSGT KQFMEALTAG ADISMIGQFG
     VGFYSAYLVA DRVTVVSKNN DDEQYIWESS AGGTFNISPD NGPSIGRGTK IILHLKDEQT
     DYLNESKIKE VIKKHSEFIS YPIYLHVQKE TEVEVPDEEA ETVEEGDDKK PKIEEVEDDE
     EDKEKKPKTK KVKEVKTEEE ELNKQKPIWT RNPQDITQEE YAAFYKSLSN DWEDHLAVKH
     FSVEGQLEFK AILFVPKRAP FDLFETKKTK NNIKLYVRRV FITDDATDLI PEWLSFVKGV
     VDSEDLPLNL SRETLQQNKI MKVIRKNIVK KALELFTEIA EDKEQFDKFY TAFSKNIKLG
     IHEDSQNRNT LAKLLRFNST KSGDEQTSLS DYVTRMPEHQ KNMYYITGES IKAVSKSPFL
     DSLKEKGFEV LFLVDPIDEY AMTQLKEFEG KKLVDITKDF ELEETEEEKK QREAEEKEYD
     GLAKALKNVL GDKVEKVVVS HKLVGAPCAI RTGQFGWSAN MERIMKAQAL RDTSMSSYMS
     SKKTFEISPK SPIIKELKQK VEADGENDKT VKSIVQLLFE TSLLVSGFTI EEPAGFAERI
     HKLVALGLNL DEEPEAAADA PAADAGVAAA ETSDNAMEEV D