ID   HSP90_EIMTE             Reviewed;         713 AA.
AC   O44001;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Heat shock protein 90;
GN   Name=HSP90;
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=PAPt38;
RA   Ouarzane M., Labbe M., Bourdieu C., Pery P.;
RL   Submitted (JAN-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; AF042329; AAB97088.1; -; mRNA.
DR   AlphaFoldDB; O44001; -.
DR   SMR; O44001; -.
DR   PRIDE; O44001; -.
DR   VEuPathDB; ToxoDB:ETH2_0701200; -.
DR   VEuPathDB; ToxoDB:ETH_00007385; -.
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..713
FT                   /note="Heat shock protein 90"
FT                   /id="PRO_0000062938"
FT   REGION          212..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           709..713
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        685..699
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   713 AA;  82413 MW;  C5E137AC8BD7B86B CRC64;
     MENKETFAFN ADIQQLMSLI INTFYSNKEI FLRELISNAS DALDKIRYEA ITEPEKLKTK
     PELFIRLIPD KANNTLTIEN SGIGMTKADL VNNLGTIARS GTKAFMEALQ AGGDISMIGQ
     FGVGFYSAYL VADSVTVVSK HNDDEQYVWE SAAGGSFTVQ KDDKYEPLGR GTRIILHLKE
     DQGEYLEERR LKDLVKKHSE FISFPIELAV EKTHEREVTE SEDEEEKKAD EKAEEKEGEE
     KKEGEEKKEG EEEKKEKTGK TKKVQEVTRE WEQLNKQKPL WMRKPEEVTE EEYASFYKSL
     SNDWEEHLAV KHFSVEGQLE FKALLFVPKR APFDLFETRK KRNNIKLYVR RVFIMDDCED
     IIPEWLNFVK GVVDSEDLPL NISRESLQQN KILKVIRKNL VKKCLEMFAE IEEKKENYAK
     FYEQFSKNLK LGIHEDSANR AKIAELLRFH SSKSGEDMVS FKEYVDRMKE GQKDIYYITG
     ESRQTVANSP FLEKLTKKGY EVLYMTDPID EYAVQQLKEF DNHKLRCCTK EGLEIDESEE
     EKKKFEELKA EFEPLLKLIK EVLHDKVDKV VLSNRITDSP CVLVTTEFGW SANMERIMKA
     QALRDNSMTS YMVSKKTMEV NGHHSIMIEI KNKAAVDKSD KTVKDLIWLL YDTALLTSGF
     SLEEPTQFAA RIHRMIKLGL SIDDDEEAKD DDLPPLEEVE GAADEASKME EVD