ID   F5ANK0_BOMMO            Unreviewed;       680 AA.
AC   F5ANK0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Heat shock protein 83 {ECO:0000256|ARBA:ARBA00021845};
DE   Flags: Fragment;
GN   Name=HSP90 {ECO:0000313|EMBL:AEB39782.1};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091 {ECO:0000313|EMBL:AEB39782.1};
RN   [1] {ECO:0000313|EMBL:AEB39782.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Pure Mysore {ECO:0000313|EMBL:AEB39782.1};
RA   Rakesh K., Manjunatha H.B., Aparna H.S.;
RT   "Bombyx mori heat shock protein 90 (BmHSP90) gene sequence from the whole
RT   body of tropical silkworm strain PM.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; HQ437671; AEB39782.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5ANK0; -.
DR   HOGENOM; CLU_006684_1_3_1; -.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd16927; HATPase_Hsp90-like; 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; 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_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 {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          25..179
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          211..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEB39782.1"
FT   NON_TER         680
FT                   /evidence="ECO:0000313|EMBL:AEB39782.1"
SQ   SEQUENCE   680 AA;  78595 MW;  EE63F990E7922C95 CRC64;
     KVETFTFQAE IAQLMSLIIN TFYSNKEIFL RELISNSSDA LDKIRYESLT DPSKLDSGKE
     LYIKIIPNKN EGTLTIIDTG IGMTKADLVN NLGTIAKSGT KAFMEALQAG ADISMIGQFG
     VGFYSSYLVA DRVTVHSKHN DDEQYVWESS AGGSFTVRPD SGEPLGRGTK IVLHVKEDLA
     EFMEEHKIKE IVKKHSQFIG YPIKLMVEKE REKELSDDEA EEEKKEEEDE KPKIEDVGED
     EDEDKKDTKK KKKTIKEKYT EDEELNKTKP IWTRNADDIT QDEYGDFYKS LTNDWEDHLA
     VKHFSVEGQL EFRALLFVPR RAPFDLFENK KRKNNIKLYV RRVFIMDNCE DLIPEYLNFI
     RGVVDSEDLP LNISREMLQQ NKILKVIRKN LVKKCLELFE ELAEDKENYK KYYEQFSKNL
     KLGIHEDSQN RAKLSELLRY HTSASGDEAC SLKEYVSRMK ENQKHIYYIT GENRDQVANS
     SFVERVKKRG YEVVYMTEPI DEYVVQQMRE YDGKTLVSVT KEGLELPEDE EEKKKREEDK
     VKFEGLCKVM KNILDNKVEK VVVSNRLVES PCCIVTAQYG WSANMERIMK AQALRDTSTM
     GYMAAKKHLE INPDHSIVET LRQKAEADKN DKAVKDLVIL LYETALLSSG FTLDEPQVHA
     SRIYRMIKLG LGIDEDEPIQ
//