ID A7XIH4_9STRA Unreviewed; 583 AA.
AC A7XIH4;
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:ABU99430.1};
DE Flags: Fragment;
GN Name=HSP90 {ECO:0000313|EMBL:ABU99430.1};
OS Phytophthora trifolii.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=54511 {ECO:0000313|EMBL:ABU99430.1};
RN [1] {ECO:0000313|EMBL:ABU99430.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PD_00168 {ECO:0000313|EMBL:ABU99430.1};
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; EU080087; ABU99430.1; -; Genomic_DNA.
DR AlphaFoldDB; A7XIH4; -.
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:ABU99430.1}.
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:ABU99430.1"
FT NON_TER 583
FT /evidence="ECO:0000313|EMBL:ABU99430.1"
SQ SEQUENCE 583 AA; 66745 MW; C3D20B4F6A274C22 CRC64;
DKNLEIKVIP DKANGTLTIQ DSGIGMTKAD LINNLGTIAK SGTKAFMEAL AAGADISMIG
QFGVGFYSAY LVADKVVVHS KHNDDEQYVW ESAAGGSFTV TPDTSEPILR GTRIVLTLKE
DMLEYLEERK LKDLVKKHSE FIGFPIKLYV EKTEEKEVTD DEEEEDEKEG EDDKPKVEEV
EEEEGEKKKK TKKIKEVTHD WDHLNSQKPI WMRKPEDVTH EEYASFYKSL TNDWEEHAGV
KHFSVEGQLE FKACLFAPKR APFDMFEGGA KKKLNNIKLY VRRVFIMDNC EELMPEYLSF
VKGVVDSEDL PLNISRETLQ QNKILRVIKK NLVKKCLEMF AELAEDNEKY NKFYEAFSKN
LKLGIHEDST NRTKIAKLLR YHSTKSGEEM TSLDDYISRM PENQPGIYYV TGESKKAVEN
SPFIEKLKKK GYEVLFMVEA IDEYAVQQLK DYEGKKLICA TKEGLKMEET EDEKKSFEEA
KAATEGLCKL MKEVLDDKVE KVEISNRIVE SPCVLVTGEY GWSANMERIM KAQALRDSST
SAYMSSKKTM EINPLHPIIK SLREKAEADK SDKTVKDLIW LLY
//
