ID A7XG64_9STRA Unreviewed; 583 AA.
AC A7XG64;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ABU99352.1};
DE Flags: Fragment;
GN Name=HSP90 {ECO:0000313|EMBL:ABU99352.1};
OS Phytophthora psychrophila.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=180901 {ECO:0000313|EMBL:ABU99352.1};
RN [1] {ECO:0000313|EMBL:ABU99352.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PD_00092 {ECO:0000313|EMBL:ABU99352.1};
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:ASU43274.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=29J6 {ECO:0000313|EMBL:ASU43274.1};
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; EU079553; ABU99352.1; -; Genomic_DNA.
DR EMBL; KX251003; ASU43274.1; -; Genomic_DNA.
DR AlphaFoldDB; A7XG64; -.
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:ABU99352.1}.
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:ABU99352.1"
FT NON_TER 583
FT /evidence="ECO:0000313|EMBL:ABU99352.1"
SQ SEQUENCE 583 AA; 66757 MW; 5A5087F27E3711F6 CRC64;
DKNLEIKVIP DKANGTLTIQ DSGIGMTKAD LINNLGTIAK SGTKAFMEAL AAGADISMIG
QFGVGFYSAY LVADKVVVHS KHNDDEQYVW ESAAGGSFTV TPDTTEPILR GTRIVLKLKE
DMLEYLEERK LKDLVKKHSE FIGFPIKLYV EKTEEKEVTD DEEEEDEKEG EDDKPKVEEV
EDEEEGEKKK KTKKIKEVTH EWDHLNSQKP IWMRKPEDVT HEEYASFYKS LTNDWEEHAG
VKHFSVEGQL EFKACLFTPK RAPFDMFEGG AKKKVNNIKL YVRRVFIMDN CEELMPEYLS
FVKGVVDSED LPLNISRETL QQNKILRVIK KNLIKKCLEM FAELAEDNEK YIKFYEAFSK
NLKLGIHEDS TNRTKIAKLL RYHSTKSGEE MTSLDDYISR MPESQPGIYY VTGESKKSVE
SSPFIEKLKK KGYEVLFMVE AIDEYAVQQL KEYEGKKLIC ATKEGLKMEE TEDEKKSFEE
AKAATEGLCK LMKEVLDDKV EKVEISNRIV ESPCVLVTGE YGWSANMERI MKAQALRDSS
TSAYMSSKKT MEINPLHPII KSLREKAEAD KSDKTVKDLI WLL
//
