ID   HSP83_DROPS             Reviewed;         717 AA.
AC   P04809; O16059; O16060; O16061; O16062; O16063; O16064; O16065; O16066;
AC   O16067; O18670; Q2M0F2;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   27-NOV-2024, entry version 169.
DE   RecName: Full=Heat shock protein 83;
DE   AltName: Full=HSP 82;
GN   Name=Hsp83; Synonyms=Hsp82; ORFNames=GA11622;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-375.
RX   PubMed=2426456; DOI=10.1016/s0022-2836(86)80001-8;
RA   Blackman R.K., Meselson M.;
RT   "Interspecific nucleotide sequence comparisons used to identify regulatory
RT   and structural features of the Drosophila hsp82 gene.";
RL   J. Mol. Biol. 188:499-515(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-269, AND VARIANTS.
RC   STRAIN=pseudo1, pseudo10, pseudo11, pseudo2, pseudo3, pseudo4, pseudo5,
RC   pseudo6, pseudo7, pseudo8, and pseudo9;
RX   PubMed=9383055; DOI=10.1093/genetics/147.3.1091;
RA   Wang R.L., Wakeley J., Hey J.;
RT   "Gene flow and natural selection in the origin of Drosophila pseudoobscura
RT   and close relatives.";
RL   Genetics 147:1091-1106(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. Required for piRNA biogenesis by facilitating
CC       loading of piRNAs into PIWI proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with shu (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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=EAL30982.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH379069; EAL30982.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X03812; CAA27439.1; -; Genomic_DNA.
DR   EMBL; AF006529; AAC07914.1; -; Genomic_DNA.
DR   EMBL; AF006530; AAC07915.1; -; Genomic_DNA.
DR   EMBL; AF006531; AAC07916.1; -; Genomic_DNA.
DR   EMBL; AF006532; AAC07917.1; -; Genomic_DNA.
DR   EMBL; AF006533; AAC07918.1; -; Genomic_DNA.
DR   EMBL; AF006534; AAC07919.1; -; Genomic_DNA.
DR   EMBL; AF006535; AAC07920.1; -; Genomic_DNA.
DR   EMBL; AF006536; AAC07921.1; -; Genomic_DNA.
DR   EMBL; AF006537; AAC07922.1; -; Genomic_DNA.
DR   EMBL; AF006538; AAC07923.1; -; Genomic_DNA.
DR   EMBL; AF006539; AAC07924.1; -; Genomic_DNA.
DR   PIR; C24827; C24827.
DR   RefSeq; XP_001353471.1; XM_001353435.3.
DR   AlphaFoldDB; P04809; -.
DR   SMR; P04809; -.
DR   STRING; 46245.P04809; -.
DR   EnsemblMetazoa; FBtr0276082; FBpp0274520; FBgn0012701.
DR   GeneID; 4813013; -.
DR   KEGG; dpo:4813013; -.
DR   CTD; 38389; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   HOGENOM; CLU_006684_1_3_1; -.
DR   InParanoid; P04809; -.
DR   OMA; MRRMKEM; -.
DR   PhylomeDB; P04809; -.
DR   ChiTaRS; Hsp83; fly.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0012701; Expressed in female reproductive system and 3 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0032991; C:protein-containing complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0097718; F:disordered domain specific binding; IEA:TreeGrafter.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0034605; P:cellular response to heat; IEA:TreeGrafter.
DR   GO; GO:0050821; P:protein stabilization; IEA:TreeGrafter.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   FunFam; 1.20.120.790:FF:000001; Heat shock protein 90 alpha; 1.
DR   FunFam; 3.30.230.80:FF:000001; Heat shock protein 90 alpha; 1.
DR   FunFam; 3.40.50.11260:FF:000001; Heat shock protein 90 alpha; 1.
DR   FunFam; 3.30.565.10:FF:000001; Heat shock protein HSP 90-alpha; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003594; HATPase_dom.
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_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..717
FT                   /note="Heat shock protein 83"
FT                   /id="PRO_0000062934"
FT   REGION          213..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           713..717
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        227..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         385
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   VARIANT         171
FT                   /note="G -> S (in strain: pseudo8 and pseudo9)"
SQ   SEQUENCE   717 AA;  81771 MW;  BF46AF2207322273 CRC64;
     MPEEAETFAF QAEIAQLMSL IINTFYSNKE IFLRELISNA SDALDKIRYE SLTDPSKLDS
     GKELYIKLIP NKTAGTLTII DTGIGMTKSD LVNNLGTIAK SGTKAFMEAL QAGADISMIG
     QFGVGFYSAY LIADRVTVTS KNNDDEQYVW ESSAGGSFTV KADNSEPLGR GTKIVLYIKE
     DQTDYLEESK IKEIVNKHSQ FIGYPIKLLV EKEREKEVSD DEADDEKKDD EAKKDMDTDE
     PKIEDVGEDE DADKKDKDGK KKKTIKEKYT EDEELNKTKP IWTRNPDDIS QEEYGEFYKS
     LTNDWEDHLC VKHFSVEGQL EFRALLFIPR RTPFDLFENQ KKRNNIKLYV RRVFIMDNCE
     DLIPEYLNFI KGVVDSEDLP LNISREMLQQ NKVLKVIRKN LVKKTMELIE ELTEDKENYK
     KFYEQFSKNL KLGVHEDSNN RAKLADFLRF HTSASGDDFC SLSDYVSRMK ENQKHVYFIT
     GESKDQVSNS AFVERVKARG FEVVYMTEPI DEYVIQHLKE YKGKQLVSVT KEGLELPEDE
     AEKKKREEDK AKFEGLCKLM KSILDSKVEK VVVSNRLVDS PCCIVTSQFG WSANMERIMK
     AQALRDTATM GYMAGKKQLE INPDHPIVEA LRQKADADKN DKAVKDLVIL LFETSLLSSG
     FSLDSPQVHA SRIYRMIKLG LGIDEDEPMT TEDAHSGGDA PGLVEDTEDA SHMEEVD
//