ID   A0A224AS81_9SOLA        Unreviewed;       699 AA.
AC   A0A224AS81;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   03-AUG-2022, entry version 18.
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}.
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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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   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   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
//