ID A7XL65_9STRA Unreviewed; 582 AA.
AC A7XL65;
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:ABU99529.1};
DE Flags: Fragment;
GN Name=HSP90 {ECO:0000313|EMBL:ABU99529.1};
OS Phytophthora phaseoli.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=129358 {ECO:0000313|EMBL:ABU99529.1};
RN [1] {ECO:0000313|EMBL:ABU99529.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PD_00067 {ECO:0000313|EMBL:ABU99529.1}, and PD_00068
RC {ECO:0000313|EMBL:ABU99530.1};
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).
RN [2] {ECO:0000313|EMBL:ASU43202.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=23B4 {ECO:0000313|EMBL:ASU43202.1}, and 35B6
RC {ECO:0000313|EMBL:ASU43203.1};
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; EU080752; ABU99529.1; -; Genomic_DNA.
DR EMBL; EU080759; ABU99530.1; -; Genomic_DNA.
DR EMBL; KX250499; ASU43202.1; -; Genomic_DNA.
DR EMBL; KX250506; ASU43203.1; -; Genomic_DNA.
DR AlphaFoldDB; A7XL65; -.
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:ABU99529.1}.
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:ABU99529.1"
FT NON_TER 582
FT /evidence="ECO:0000313|EMBL:ABU99529.1"
SQ SEQUENCE 582 AA; 66715 MW; FC7B1FE6A0E98937 CRC64;
DKNLEIKVIP DKANGTLTIQ DSGIGMTKAD LINNLGTIAK SGTKAFMEAL AAGADISMIG
QFGVGFYSAY LVADKVVVHS KHNDDEQYVW ESAAGGSFTV TPDTSEPIQR GTRIVLKLKE
DMLEYLEERK LKDLVKKHSE FIGFPIKLYV EKTEEKEVTD DEEEEDEKEV EDDKPKVEEV
EEEEGEKKKK TKKIKEVTHE WDHLNSQKPI WMRKPEDVTH EEYASFYKSL TNDWEEHAGV
KHFSVEGQLE FKACLFTPKR APFDMFEGGA KKKVNNIKLY VRRVFIMDNC EELMPEYLSF
VKGVVDSEDL PLNISRETLQ QNKILRVIKK NLVKKCLEMF AELAEDNEKY NKFYESFSKN
LKLGIHEDST NRTKIAKLMR YHSTKSGEEV TSLDDYISRM PESQPGIYYV TGESKKSVEN
SPFIEKLKKK GYEVLFMVEA IDEYAVQQLK EYEGKKLICA TKEGLKMEET EDEKKSFEEA
KAATEGLCKL MKEVLDDKVE KVEISNRIVE SPCVLVTGEY GWSANMERIM KAQALRDSST
SAYMTSKKTM EINPLHPIIK SLREKAEADK SDKTVKDLIW LL
//
