ID   I4CFF7_9STRA            Unreviewed;       297 AA.
AC   I4CFF7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:AFM28343.1};
DE   Flags: Fragment;
GN   Name=HSP90 {ECO:0000313|EMBL:AFM28343.1};
OS   Phytophthora gonapodyides.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=78237 {ECO:0000313|EMBL:AFM28343.1};
RN   [1] {ECO:0000313|EMBL:AFM28343.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TAS35 {ECO:0000313|EMBL:AFM28343.1};
RA   Aghighi S., Hardy G.E.S.J., Scott J.K., Burgess T.I.;
RT   "Phytophthora bilorbang sp. nov., a new species associated with the decline
RT   of Rubus anglocandicans (European blackberry) in Western Australia.";
RL   Eur. J. Plant Pathol. 133:841-855(2012).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; JN547653; AFM28343.1; -; Genomic_DNA.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
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   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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:AFM28343.1}.
FT   REGION          149..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..173
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFM28343.1"
FT   NON_TER         297
FT                   /evidence="ECO:0000313|EMBL:AFM28343.1"
SQ   SEQUENCE   297 AA;  33996 MW;  1E168B9726B2126C CRC64;
     KVIPDKANGT LTIQDSGIGM TKADLINNLG TIAKSGTKAF MEALAAGADI SMIGQFGVGF
     YSAYLVADKV VVHSKHNDDE QYVWESAAGG SFTVTPDTTE PILRGTRIVL KLKEDMLEYL
     EERKLKDLVK KHSEFIGFPI KLYVEKTEEK EVTDDEEEED EKEGEDDKPK VEEVEEEEGE
     KKKKTKKIKE VTHEWDHLNS QKPIWMRKPE DVTHEEYASF YKSLTNDWEE HAXVKHFSVE
     GQLEFKACLF TPKRAPFDMF EGGAKKKINN IKLYVRRVFI MDNCEELMPE YLSFVKG
//