ID Q6VNX1_DRONE Unreviewed; 345 AA.
AC Q6VNX1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Heat shock protein 83 {ECO:0000256|ARBA:ARBA00021845};
DE AltName: Full=HSP 82 {ECO:0000256|ARBA:ARBA00029975};
DE Flags: Fragment;
GN Name=Hsp83 {ECO:0000313|EMBL:AAR05877.1,
GN ECO:0000313|FlyBase:FBgn0068805};
OS Drosophila nebulosa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7271 {ECO:0000313|EMBL:AAR05877.1};
RN [1] {ECO:0000313|EMBL:AAR05877.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Drosophila Resource Center 14030-0761.0
RC {ECO:0000313|EMBL:AAR05877.1};
RX PubMed=15008418; DOI=10.1007/s00239-003-0030-3;
RA Powell J.R., Sezzi E., Moriyama E.N., Gleason J.M., Caccone A.;
RT "Analysis of a shift in codon usage in Drosophila.";
RL J. Mol. Evol. 57:S214-S225(2003).
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; AY335221; AAR05877.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6VNX1; -.
DR FlyBase; FBgn0068805; Dneb\Hsp83.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
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 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; 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};
KW Stress response {ECO:0000313|EMBL:AAR05877.1}.
FT DOMAIN 15..169
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 200..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAR05877.1"
FT NON_TER 345
FT /evidence="ECO:0000313|EMBL:AAR05877.1"
SQ SEQUENCE 345 AA; 39390 MW; 7748B0C59B907A3D CRC64;
IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT DSSKLESGKE LYIKLIPNKT
AGTLTIIDTG IGMTKSDLVN NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA
DKVTVTSKNN DDEQYIWESS AGGSFTVKAD NSEPLGRGTK IVLYIKEDQT DYLEESKIKE
IVNKHSQFIG YPIKLLVEKE REKEVSDDEA DDETKEGDDK EKKEMDTDEP KIEDVGEDED
ADKKEGDAKK KKTIKEKYTE DEELNKTKPI WTRNPDDISQ EEYGEFYKSL TNDWEDHLAV
KHFSVEGQLE FRALLFIPRR TPFDLFENQK KRNNIKLYVR RVFIM
//
