ID D5KXW7_NILLU Unreviewed; 730 AA.
AC D5KXW7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Heat shock protein 83 {ECO:0000256|ARBA:ARBA00021845};
GN Name=hsp90 {ECO:0000313|EMBL:ADE34169.1};
OS Nilaparvata lugens (Brown planthopper).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Delphacinae; Nilaparvata.
OX NCBI_TaxID=108931 {ECO:0000313|EMBL:ADE34169.1};
RN [1] {ECO:0000313|EMBL:ADE34169.1}
RP NUCLEOTIDE SEQUENCE.
RA Lu K., Zhou Q.;
RT "Molecular characterization and expression pattern of the heat shock
RT protein 90 (hsp90) from Nilaparvata lugens.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APA34047.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NlSFP_unconfirmed_comp28726 {ECO:0000313|EMBL:APA34047.1};
RX PubMed=27538518; DOI=10.1186/s12864-016-3013-7;
RA Yu B., Li D.T., Lu J.B., Zhang W.X., Zhang C.X.;
RT "Seminal fluid protein genes of the brown planthopper, Nilaparvata
RT lugens.";
RL BMC Genomics 17:654-654(2016).
RN [3] {ECO:0000313|EMBL:QOC60280.1}
RP NUCLEOTIDE SEQUENCE.
RA Chen X., Li Z.-d., Dai Y.-T., Jiang M.-X., Zhang C.-X.;
RT "Identification and characterization of 3 heat shock protein 90 (Hsp90)
RT homologs in the brown planthopper.";
RL Submitted (MAR-2020) 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; GU723300; ADE34169.1; -; mRNA.
DR EMBL; KU932411; APA34047.1; -; mRNA.
DR EMBL; MT221445; QOC60280.1; -; mRNA.
DR AlphaFoldDB; D5KXW7; -.
DR SMR; D5KXW7; -.
DR EnsemblMetazoa; XM_022347057.2; XP_022202749.1; LOC111059404.
DR OrthoDB; 547579at2759; -.
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 2: Evidence at transcript level;
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:ADE34169.1}.
FT DOMAIN 35..189
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 221..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 83806 MW; C1E6295483F59857 CRC64;
MPEDVQMEAG EVETFVFQAE IAQLMSLIIN TFYSNKEIFL RELISNSSDA LDKIRYEGLT
DASKLESGKD LQIKIIPNKN DRTLTIIDTG IGMTKADLVN NLGTIAKSGT KAFMEALQAG
ADISMIGQFG VGFYSAYLVA DKVTVTSKHN DDEQYLWESS AGGSFTVRPD HTEPLGRGTK
IVLYIKEDQA EFLEERKIKE VVKKHSQFIG YPIKLLVEKE RDKELSDDEA DEEEQEEKKK
EGEGDKAEDE EDKTPKIEDV EDEGEDGEKK KKKKKTVKEK YTEDEELNKT KPIWTRNSDD
IGQEEYGEFY KSLTNDWEDH LAVKHFSVEG QLEFRALLFV PRRAPFDLFE NKKRKNNIKL
YVRRVFIMDN CEDLIPEYLN FIKGVVDSED LPLNISREML QQNKILKVIR KNLVKKCLEL
FEELAEDKDN YKKFYEQFSK NLKLGIHEDS QNRKKLSDLL RYHTSASGDD NCSLKDYVGR
MKENQKHIYY ITGESKDQVA NSSFVELVKK RGFEVVYMTE PIDEYVVQQM KEYDGKQLVS
VTKEGLELPE DEAEKKKRED DKAKFENLCK VMKDILDKKV EKVVVSNRLV ESPCCIVTSQ
YGWTANMERI MKAQALRDTS TMGYMAAKKH LEINPDHSII DTLRTKADED KNDKAVKDLV
MLLFETALLS SGFALEDPGV HAARIHRMIK LGLCIEEDDP VPHDDEKVDA EMPPLEGEAS
EDASRMEEVD
//
