ID A0A224AS81_9SOLA Unreviewed; 699 AA. AC A0A224AS81; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 29-SEP-2021, entry version 16. 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 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 1.20.120.790; -; 1. DR Gene3D; 3.30.565.10; -; 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_S5_D2-typ_fold. DR PANTHER; PTHR11528; PTHR11528; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00183; HSP90; 1. DR PIRSF; PIRSF002583; Hsp90; 1. DR PRINTS; PR00775; HEATSHOCK90. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF110942; SSF110942; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Stress response {ECO:0000313|EMBL:BBA20380.1}. FT DOMAIN 27..182 FT /note="HATPase_c" 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 COILED 522..542 FT /evidence="ECO:0000256|SAM:Coils" 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 //