ID F4MJM2_BACOL Unreviewed; 666 AA.
AC F4MJM2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative heat shock protein 83 {ECO:0000313|EMBL:CAY56585.1};
DE Flags: Fragment;
GN Name=hsp83 {ECO:0000313|EMBL:CAY56585.1};
OS Bactrocera oleae (Olive fruit fly) (Dacus oleae).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Bactrocera; Daculus.
OX NCBI_TaxID=104688 {ECO:0000313|EMBL:CAY56585.1};
RN [1] {ECO:0000313|EMBL:CAY56585.1}
RP NUCLEOTIDE SEQUENCE.
RA Vartholomaiou E., Pantzartzi C.N., Drosopoulou E., Scouras Z.G.;
RT "The hsp83 gene of Bactrocera oleae.";
RL Submitted (MAY-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; FN392227; CAY56585.1; -; Genomic_DNA.
DR AlphaFoldDB; F4MJM2; -.
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 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; 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; PF13589; HATPase_c_3; 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:CAY56585.1}.
FT REGION 172..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAY56585.1"
FT NON_TER 666
FT /evidence="ECO:0000313|EMBL:CAY56585.1"
SQ SEQUENCE 666 AA; 76218 MW; AC4969ED2BF46535 CRC64;
DALDKIRYES LTDPTKLDSG KELYIKLIPN KTAGTLTIID TGIGMTKSDL VNNLGTIAKS
GTKAFMEALQ AGADISMIGQ FGVGFYSAYL VADKVTVTSK HNDDEQYIWE SSAGGSFTVK
PDNTEPLGRG TKIVLYIKED QTEYLEESKI KEIVNKHSQF IGYPIKLLVE KERDQEVSDD
EAEDDKKDEE KKDMDTDEPK IEDVGEDDDA DKDKDKKKKK TVKVKYTEDE ELNKTKPIWT
RNPDDISQEE YDEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRTP FDLFENQKKR
NNIKLYVRRV FIMDNCEELI PEYLNFIKGV VDSEDLPLNI SREMLQQNKV LKVIRKNLVK
KTMELIEELT EDKELYKKFY DQFAKNLKLG VHEDSNNRAK LADFLRYHTS ASGDDAASLS
DYVSRMKSNQ RHIYFITGES KEQVSNSAFV ERVKARGFEV IYMTEPIDEY VIQHLKEYKG
KQLTSVTKEG LELPEDEAEK KKREEDKAKF ENLCKLMKSI LDNKVEKVVV SNRLVESPCC
IVTSQFGWSA NMERIMKAQA LRDTSTMGYM AGKKHLEINP EHPIIETLRQ KAEADKDDKA
VKDLCILLFE TALLSSGFSL DSPQVHASRI YRMIKLGLGI DEEEPMATED TQSGGDAPPL
VDDTED
//
