ID A8B078_9STRA Unreviewed; 582 AA.
AC A8B078;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ABU99439.1};
DE Flags: Fragment;
GN Name=HSP90 {ECO:0000313|EMBL:ABU99439.1};
OS Phytophthora sp. P7491.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=467792 {ECO:0000313|EMBL:ABU99439.1};
RN [1] {ECO:0000313|EMBL:ABU99439.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PD_00395 {ECO:0000313|EMBL:ABU99439.1};
RX PubMed=18039586; DOI=10.1016/j.fgb.2007.10.010;
RA Blair J.E., Coffey M.D., Park S.Y., Geiser D.M., Kang S.;
RT "A multi-locus phylogeny for Phytophthora utilizing markers derived from
RT complete genome sequences.";
RL Fungal Genet. Biol. 45:266-277(2008).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; EU080150; ABU99439.1; -; Genomic_DNA.
DR AlphaFoldDB; A8B078; -.
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; 3.40.50.11260; -; 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:ABU99439.1}.
FT REGION 155..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABU99439.1"
FT NON_TER 582
FT /evidence="ECO:0000313|EMBL:ABU99439.1"
SQ SEQUENCE 582 AA; 66626 MW; C6B3851196BCBD16 CRC64;
DKNLEIKVIP DKANGTLTIQ DSGIGMTKAD LINNLGTIAK SGTKAFMEAL AAGADISMIG
QFGVGFYSAY LVADKVVVHS KHNDDEQYVW ESAAGGSFTV TPDTTEPILR GTRIVLTLKE
DMLEYLEERK LKDLVKKHSE FIGFPIKLYV EKTEEKEVTD DEEEEDEKEG EDDKPKVEEV
EDEEGEKKKK TKKIKEVTHE WDHLNSQKPI WMRKPEDVTH EEYASFYKSL TNDWEEHAGV
KHFSVEGQLE FKACLFAPKR APFDMFEGGA KKKLNNIKLY VRRVFIMDNC EELMPEYLSF
VKGVVDSEDL PLNISRETLQ QNKILRVIKK NLVKKCLEMF AELAEDNEKY NKFYEAFSKN
LKLGIHEDST NRTKIAKLLR YHSTKSGEEM TSLDDYISRM PENQPGIYYV TGESKKSVEN
SPFIEKLKKK GYEVLFMVEA IDEYAVQQLK EYEGKKLICA TKEGLKMEET EDEKKSFEEA
KAATEGLCKL MKEVLDDKVE KVEISNRIVE SPCVLVTGEY GWSANMERIM KAQALRDSST
SAYMSSKKTM EINPLHPIIK SLREKAEADK SDKTVKDLIW LL
//
