ID   C9E0R6_9APIC            Unreviewed;       594 AA.
AC   C9E0R6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ACV71143.1};
DE   Flags: Fragment;
GN   Name=hsp90 {ECO:0000313|EMBL:ACV71143.1};
OS   Babesia sp. Hebei.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=462222 {ECO:0000313|EMBL:ACV71143.1};
RN   [1] {ECO:0000313|EMBL:ACV71143.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hebei {ECO:0000313|EMBL:ACV71143.1};
RA   Guan G., Yin H., Chauvin A., Luo J., Moreau E.;
RT   "Molecular characterization of a member of hsp90 gene family from Babesia
RT   sp. BQ1 (Lintan) infective to small ruminants in China.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; GQ443605; ACV71143.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9E0R6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0051082; F:unfolded protein binding; IEA:InterPro.
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   InterPro; IPR036890; HATPase_C_sf.
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; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Stress response {ECO:0000313|EMBL:ACV71143.1}.
FT   REGION          91..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACV71143.1"
SQ   SEQUENCE   594 AA;  68984 MW;  DCB2168254FF8D3F CRC64;
     GVGFYSAYLV ADKVTVVSKN NNDDQYMWES SASGHFTVTK DESGEQLKRG TRLILHLKDD
     QGEYLEERRL KDLVKKHSEF ISFPIRLSVE KTTETEVTDD EAEAPTPAES KDEEKIKDVT
     DEAEKEGEEA KEGEDKEGDK TAEKKKRKVT SVTREWEMLN KQKPIWMRLP TEVTHEEYAS
     FYKNLCNDWE DHLAVKHFSV EGQLEFKALL FIPKRAPFDM FESRKKKNNI KLYVRRVFIM
     DDCEELIPEW LGFVKGVVDS EDLPLNISRE ILQQNKILKV IRKNLVKKCL ELFSELTEKK
     EDFKKFYEQF SKNLKLGIHE DNANRTKIAE LLRYETSKSG DEAISLKEYV DRMKPDQKYI
     YYITGESKQS VANSPFLEVL RSKGIEVIYM TDPIDEYAVQ QIKEFEGKKL KCCTKENLEL
     EDTEEERKSF ETLQKEMEPL CRVIKEILHD KVEKVVCGKR FTESPCALVT SEFGWSANME
     RIMKAQALRD NNFGSFMISK KTMELNPHHS IMKELKQRAE ADKSDKTLKD LVWLLYDTAI
     LTSGFNLDDP TQFGGRIYRM IKLGLSLDDD AAVEDVEIPS LDEVVVDPKM EEVD
//