ID   HSP83_LEIAM             Reviewed;         701 AA.
AC   P27741;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Heat shock protein 83;
DE            Short=HSP 83;
GN   Name=HSP83;
OS   Leishmania amazonensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/BR/77/LTB0016/C1S1;
RX   PubMed=2270107; DOI=10.1016/0166-6851(90)90168-l;
RA   Shapria M., Pedraza G.;
RT   "Sequence analysis and transcriptional activation of heat shock protein 83
RT   of Leishmania mexicana amazonensis.";
RL   Mol. Biochem. Parasitol. 42:247-256(1990).
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.
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; M92926; AAA29250.1; -; Genomic_DNA.
DR   PIR; A44943; A44943.
DR   AlphaFoldDB; P27741; -.
DR   SMR; P27741; -.
DR   VEuPathDB; TriTrypDB:LAMA_000120800; -.
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; Stress response.
FT   CHAIN           1..701
FT                   /note="Heat shock protein 83"
FT                   /id="PRO_0000062939"
FT   REGION          211..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           697..701
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        227..248
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;  80585 MW;  05100A1324A80812 CRC64;
     MTETFAFQAE INQLMSLIIN TFYSNKEIFL RDVISNASDA CDKIRYQSLT DPSVLGDATR
     LCVRVVPDKE NKTLTVEDNG IGMTKADLVN NLGTIARSGT KAFMEALEAG ADMSMIGQFG
     VGFYSAYLVA DRVTVTSKNN SDEVYVWESS AGGTFTITSA PESDMKLPAR ITLHLKEDQL
     EYLEARRLKE LIKKHSEFIG YDIELMVEKT TEKEVTDEDE EEAKKADEDG EEPKVEEVTE
     GEEGKKKKTK KVKEVTKEYE VQNKHKPLWT RDPKDVTKEE YAAFYKAISN DWEDPPATKH
     FSVEGQLEFR AIMFVPKRAP FDMLEPNKKR NNIKLYVRRV FIMDNCEDLC PDWLGFVKGV
     VDSEDLPLNI SRENLQQNKI LKVIRKNIVK KCLEMFEEVA ENKEDYKQFY EQFGKNIKLG
     IHEDTANRKK LMELLRFYST ESGEVMTTLK DYVTRMKAEQ NSIYYITGDS KKKLESSPFI
     EQAKRRGFEV LFMTEPYDEY VMQQVKDFED KKFACLTKEG VHFEESEEEK RQREEEKATC
     EKLCKTMKEV LGDKVEKVTV SERLSTSPCI LVTSEFGWSA HMEQMMRNQA LRDSSMAQYM
     MSKKTMELNP KHPIIKELRR RVEADENDKA VKDLVFLLFD TSLLTSGFQL EDPTYAERIN
     RMIKLGLSLD EEEEEEAVEA AVAETAPAEV TAGTSSMELV D