ID A0A224AS81_9SOLA Unreviewed; 699 AA. AC A0A224AS81; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 24-JAN-2024, entry version 23. DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:BBA20380.1}; GN Name=HSP90 {ECO:0000313|EMBL:BBA20380.1}; OS Nicotiana gossei. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=118698 {ECO:0000313|EMBL:BBA20380.1}; RN [1] {ECO:0000313|EMBL:BBA20380.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NgHSP90_1 {ECO:0000313|EMBL:BBA20379.1}, and NgHSP90_2 RC {ECO:0000313|EMBL:BBA20380.1}; RA Mino M., Katsuyama Y., Doi M., Okumura H., Ikusawa R., Takada R., RA Kitajima S., Oda K., Sato K., Tanaka Y., Tezuka T.; RT "A possible role of chaperon complex protein genes for disease resistant RT proteins in speciation processes in genus Nicotiana."; RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. CC {ECO:0000256|ARBA:ARBA00008239}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LC314274; BBA20379.1; -; mRNA. DR EMBL; LC314275; BBA20380.1; -; mRNA. DR AlphaFoldDB; A0A224AS81; -. 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:SF138; HEAT SHOCK COGNATE PROTEIN 80; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Stress response {ECO:0000313|EMBL:BBA20380.1}. FT DOMAIN 27..182 FT /note="Histidine kinase/HSP90-like ATPase" FT /evidence="ECO:0000259|SMART:SM00387" FT REGION 219..248 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 670..699 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 219..238 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 672..699 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 699 AA; 80158 MW; 14D1463153A79DAA CRC64; MAEAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES LTDKSKLDAQ PELFIHIIPD KTNNSLTIID SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ FGVGFYSAYL VAEKVIVTTK HNDDEQYVWE SQAGGSFTVT RDTSGENLGR GTKITLFLKE DQLEYLEERR LKDLIKKHSE FISYPISLWV EKTIEKEISD DEEEEEKKDE EGKVEEVDEE KEKEEKKKKK VKEVSNEWSL VNKQKPIWMR KPDEITKEEY AAFYKSLTND WEEHLAVKHF SVEGQLEFKA ILFVPKRAPF DLFDTRKKPN NIKLYVRRVF IMDNCEELIP EYLSFVKGIV DSEDLPLNIS REMLQQNKIL KVIRKNLVKK CVELFFEIAE NKEDYNKFYE AFSKNLKLGI HEDSQNRSKF AELLRYHSTK SGDEMTSLKD YVTRMKEGQN DIYYITGESK KAVENSPFLE KLKKKGYEVL YMVDAIDEYS IGQLKEFEGK KLVSATKEGL KLDESEDEKK KQEELKEKFE GLCKVIKDVL GDKVEKVVVS DRVVDSPCCL VTGEYGWTAN MERIMKAQAL RDSSMAGYMS SKKTMEINPE NAIMEELRKR ADADKNDKSV KDLVLLLFET ALLTSGFSLE EPNTFGNRIH RMLKLGLSID EDSGDADADM PALEDPEADA EGSKMEEVD //