ID A7XJT3_9STRA Unreviewed; 580 AA. AC A7XJT3; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 24-JAN-2024, entry version 63. DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ABU99482.1}; DE Flags: Fragment; GN Name=HSP90 {ECO:0000313|EMBL:ABU99482.1}; OS Elongisporangium undulatum. OC Eukaryota; Sar; Stramenopiles; Oomycota; Pythiales; Pythiaceae; OC Elongisporangium. OX NCBI_TaxID=127444 {ECO:0000313|EMBL:ABU99482.1}; RN [1] {ECO:0000313|EMBL:ABU99482.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PD_01122 {ECO:0000313|EMBL:ABU99482.1}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU080443; ABU99482.1; -; Genomic_DNA. DR AlphaFoldDB; A7XJT3; -. 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:ABU99482.1}. FT REGION 155..194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 156..177 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 178..194 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABU99482.1" FT NON_TER 580 FT /evidence="ECO:0000313|EMBL:ABU99482.1" SQ SEQUENCE 580 AA; 66163 MW; CFDEEDD29121A767 CRC64; DKNLEIKIIP DKANGTLTLQ DSGIGMTKAD LINNLGTIAK SGTKAFMEAL AAGADISMIG QFGVGFYSAY LVADKVVVHS KHNDDEQYVW ESAAGGSFTV TPDTSEPIPR GTRIVLKLKE DMLEYLEERK LKDLVKKHSE FIGFPIKLYV EKTEEKEVTD DEEEEEEADD DKPKVEEVDE EEGEKKKKTK KIQEVSHDWN HLNSQKPIWM RKPEDVTHEE YAAFYKSLTN DWEEHAAVKH FSVEGQLEFK ACLYAPKRAP FDMFEGGAKK KLNNIKLYVR RVFIMDNCEE LMPEYLSFVK GVVDSEDLPL NISRETLQQN KILRVIKKNL VKKCLEMFAE LAEDNEKYSK FYEAFSKNLK LGIHEDSTNR TKIAKLLRYH STKSGEEMTS LDDYISRMPE NQPGIYYVTG ESKKAVETSP FIEKLKKKGY EVIYMVEAID EYAVQQLKEY EGKKLISATK EGLAMEESEE EKKTFEEAKA ATAGLCKLMK EVLDDKVEKV EVSNRIVESP CVLVTGEYGW SANMERIMKA QALRDSSTGA YMSSKKTMEI NPLHPIIKSL REKAEADKSD KTVKDLVWLL //