ID G0WKT0_BURMU Unreviewed; 708 AA.
AC G0WKT0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ADK26462.1};
GN Name=Hsp90 {ECO:0000313|EMBL:ADK26462.1};
OS Bursaphelenchus mucronatus (Pinewood nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC Bursaphelenchus.
OX NCBI_TaxID=6325 {ECO:0000313|EMBL:ADK26462.1};
RN [1] {ECO:0000313|EMBL:ADK26462.1}
RP NUCLEOTIDE SEQUENCE.
RA Peng D.L., Dai L.L., Ge J.J., Li H.M.;
RT "Cloning, characterization and function analysis of a new heat shock
RT protein 90 gene (Bmnj-hsp90-1) from Bursaphelenchus mucronatus.";
RL Submitted (MAY-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; HM347331; ADK26462.1; -; mRNA.
DR AlphaFoldDB; G0WKT0; -.
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:ADK26462.1}.
FT DOMAIN 29..183
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 216..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 81624 MW; 4094C31E060052A7 CRC64;
MSEQKEETFA FQAEIAQLMS LIINTFYSNK EIFLRELISN SSDALDKIRY QALTEPQELE
TGKELYIKIT PNKAEKTLTI MDTGIGMTKA DLVNNLGTIA KSGTKAFMEA LQAGADISMI
GQFGVGFYSA FLVADRVVVT SKHNDDETYE WESSAGGSFI IRQVQDPELT RGTKIVLHIK
EDQTEYLEER RIKEIVKKHS QFIGYPIKLV VEKEREKEVE DDEAEEKEEK KDEEKKEGEI
EEDKDEEKKD EKKTKKIKEK YLEDEELNKT KPIWTRNPDD ISNEEYAEFY KSLSNDWEDH
LAVKHFSVEG QLEFRALLFV PQRAPFDLFE NKKAKNSIKL YVRRVFIMEN CDELMPDYLN
FIKGVVDSED LPLNISRETL QQSKILKVIR KNLIKKCMEL FSEIAEDKDN FKKFYEQFGK
NIKLGIHEDS TNRKKLAEFL RYHTSTSGDE TSSLQDYVSR MKENQTAIYY ITGESREAVA
NSAFVERVKK RGFEVVYMVD PIDEYCVQQL KEFDGKKLVS VTREGLELPE SEEEKKKFEE
DKVKFEKLCK VMKDILDKKV QKVSVSNRLV SSPCCIVTSE YGWSANMERI MKAQALRDSS
TMGYMASKKN LEINPDHSIM KALRERVEND QDDKTARDLV VLLFETALLT SGFSLEEPGS
HANRIFRMIK LGLDIDEADA VEESTSAPVE VPKVEGAEED ASRMEEVD
//
