ID   A0A288ZA70_PHYBB        Unreviewed;       583 AA.
AC   A0A288ZA70;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ASU43418.1};
DE   Flags: Fragment;
OS   Phytophthora brassicae.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=187813 {ECO:0000313|EMBL:ASU43418.1};
RN   [1] {ECO:0000313|EMBL:ASU43418.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=61J8 {ECO:0000313|EMBL:ASU43418.1};
RA   Yang X., Tyler B.M., Hong C.;
RT   "An expanded multi-locus phylogeny for the genus Phytophthora with new
RT   insights into its evolutionary history.";
RL   Submitted (MAY-2016) 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; KX252004; ASU43418.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A288ZA70; -.
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   InterPro; IPR036890; HATPase_C_sf.
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   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.
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:ASU43418.1}.
FT   REGION          155..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..180
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ASU43418.1"
FT   NON_TER         583
FT                   /evidence="ECO:0000313|EMBL:ASU43418.1"
SQ   SEQUENCE   583 AA;  66646 MW;  EDF0F89EDA730287 CRC64;
     DKNLEIKVIP DKANGTLTIQ DSGIGMTKAD LINNLGTIAK SGTKAFMEAL AAGADISMIG
     QFGVGFYSAY LVADKVVVHS KHNDDEQYVW ESAAGGSFTV TPDTTEPILR GTRIVLTLKE
     DMLEYLEERK LKDLVKKHSE FIGFPIKLYV EKTEEKEVTD DEEEEDEKEG EDDKPKVEEV
     EDEEEGEKKK KTKKIKEVTH EWDHLNSQKP IWMRKPEDVT HEEYASFYKS LTNDWEEHAG
     VKHFSVEGQL EFKACLFAPK RAPFDMFEGG AKKKLNNIKL YVRRVFIMDN CEDLMPEYLS
     FVKGVVDSED LPLNISRETL QQNKILRVIK KNLVKKCLEM FAELAEDNEK YSKFYEAFSK
     NLKLGIHEDS TNRTKIAKLL RYHSTKSGEE TTSLDDYISR MPETQPGIYY VTGESKKSVE
     SSPFIEKLKK KGYEVIFMID AIDEYAVQQL KEYEGKKLIC ATKEGLKMEE TEDEKKSFEE
     AKAATEGLCK LMKEVLDDKV EKVEISNRIV ESPCVLVTGE YGWSANMERI MKAQALRDSS
     TSSYMSSKKT MEINPLHPII NSLREKAEAD KSDKTVKDLI WLL
//