ID   HSP82_AJECA             Reviewed;         679 AA.
AC   P33125;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Heat shock protein 82;
GN   Name=HSP82;
OS   Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=5037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26034 / G222B;
RX   PubMed=1581351; DOI=10.1016/0167-4781(92)90106-a;
RA   Minchiotti G., Gargano S., Maresca B.;
RT   "Molecular cloning and expression of hsp82 gene of the dimorphic pathogenic
RT   fungus Histoplasma capsulatum.";
RL   Biochim. Biophys. Acta 1131:103-107(1992).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33383.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M55629; AAA33383.1; ALT_FRAME; Genomic_DNA.
DR   PIR; S21764; S21764.
DR   AlphaFoldDB; P33125; -.
DR   SMR; P33125; -.
DR   PRIDE; P33125; -.
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; -; 2.
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; Stress response.
FT   CHAIN           1..679
FT                   /note="Heat shock protein 82"
FT                   /id="PRO_0000062959"
FT   REGION          216..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           675..679
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        228..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         373
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   679 AA;  77417 MW;  C1066E8DC4A956A7 CRC64;
     MSSETFEFQA EISQLLSLII NTVYSNKEIF LRELISNFSD ALDKIRYKAL SDPSKLESDK
     DLRIDITPDK ENKTLTIRDT GIGMTKADLV NNLGTIARSG TKQFMEALTA GADISMIGQF
     GVGFYSAYLV ADKVTVISKS NDDEQYIWES NAGGTFKVTQ DDDGRAIGRG TKMILHLKDE
     QTEYLNESKI KEVVKKQSEF IFYPIYLHVL KENEKEVPDE DAEEVKDEGD DKAPKVEEVD
     EDEEDKTKAK KTKKIKENKI EEEELNKTKP IWTRNPADIT QEEYASFYKT NDWEDHLAVK
     HFSVEGQLEF RAILFVPKRA PFDLFETKKT KNNIKLYVRR VFITDDATDL IPEWLSFIKG
     VVDSEDLPLG LSRETLQQNK IMKVIKNIVK KTLELFNEIA EDREQFDKFY SAFSKNIKLG
     VHEDAQNRPA LAKLLRYNST KSGDETTSLT DYVTRMPEHH KTIYYITGES LKAVQKSPFL
     DTLKEKNFEV LFLVDPNDEY AMTQLKEFDG KKLVDITKDF ELEETEEEKK DREAEEKEYE
     GLAKSLENIL GDKVEKVVVS HKLIGSPCAI RTGQFGWSAN MERIMKAQAL RDTSMSSRRS
     SRPTEGNDRT VKSITQLLFE TSLLVSGFTI EEPSGFAGRI HKLVSLGLNI DEDAETSEEK
     EADTVVAEAP ADSDMEEVD