ID A7XKX4_9STRA Unreviewed; 582 AA.
AC A7XKX4;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ABU99516.1};
DE Flags: Fragment;
GN Name=HSP90 {ECO:0000313|EMBL:ABU99516.1};
OS Phytophthora cuyabensis.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=445396 {ECO:0000313|EMBL:ABU99516.1};
RN [1] {ECO:0000313|EMBL:ABU99516.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PD_01117 {ECO:0000313|EMBL:ABU99516.1};
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; EU080668; ABU99516.1; -; Genomic_DNA.
DR AlphaFoldDB; A7XKX4; -.
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 HAMAP; MF_00505; HSP90; 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:ABU99516.1}.
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:ABU99516.1"
FT NON_TER 582
FT /evidence="ECO:0000313|EMBL:ABU99516.1"
SQ SEQUENCE 582 AA; 66555 MW; 44E98904D4881EB6 CRC64;
DKNLEIKVIP DKANGTLTIQ DSGIGMTKAD LINNLGTIAK SGTKAFMEAL AAGADISMIG
QFGVGFYSAY LVADKVVVHS KHNDDEQYVW ESAAGGSFTV TPDTSEPIAR GTRIVLKLKE
DMLEYLEERK LKDLVKKHSE FIGFPIKLYV EKTEEKEVTD DEEDEDEKEG DDDKPKVEEV
DEEEGEKKKK TKKIKEVTHE WDHLNSQKPI WMRKPEDVTH EEYASFYKSL TNDWEEHAAV
KHFSVEGQLE FKACLFTPKR APFDMFEGGA KKKLNNIKLY VRRVFIMDNC EELMPEYLSF
VKGVVDSEDL PLNISRETLQ QNKILRVIKK NLVKKCLEMF AELAEDSEKY NKFYEAFSKN
LKLGIHEDST NRTKIAKLLR YHSTKSGEEM TSLDDYISRM PENQPGIYYV TGESKKSVEN
SPFIEKLKKK GYEVLFMVEA IDEYAVQQLK EYEGKKLICA TKEGLKMDES EDEKKAFEEA
KAATEGLCKL MKEVLDDKVE KVQISNRIVE SPCVLVTGEY GWSANMERIM KAQALRDSST
SAYMTSKKTM EINPLHPIIK SLREKAEADK SDKTVKDLIW LL
//
