ID A1C289_9EUKA Unreviewed; 569 AA.
AC A1C289;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ABL11319.1};
DE Flags: Fragment;
GN Name=hsp90 {ECO:0000313|EMBL:ABL11319.1};
OS uncultured Oxymonadida sp.
OC Eukaryota; Metamonada; Preaxostyla; Oxymonadida; environmental samples.
OX NCBI_TaxID=413579 {ECO:0000313|EMBL:ABL11319.1};
RN [1] {ECO:0000313|EMBL:ABL11319.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18211267; DOI=10.1111/j.1462-2920.2007.01430.x;
RA de Koning A.P., Noble G.P., Heiss A.A., Wong J., Keeling P.J.;
RT "Environmental PCR survey to determine the distribution of a non-canonical
RT genetic code in uncultivable oxymonads.";
RL Environ. Microbiol. 10:65-74(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; DQ925170; ABL11319.1; -; Genomic_DNA.
DR AlphaFoldDB; A1C289; -.
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; IPR003594; HATPase_C.
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 SMART; SM00387; HATPase_c; 1.
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:ABL11319.1}.
FT DOMAIN 2..157
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 191..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL11319.1"
FT NON_TER 569
FT /evidence="ECO:0000313|EMBL:ABL11319.1"
SQ SEQUENCE 569 AA; 66273 MW; 5FB9D85FF3C8846B CRC64;
SNKDIFLREL ISNASDALDK IRYRSLTDKA LLEEEPRFEI RLIPDKVNKI LHICDTGVGM
TETELVNNLG TIASSGTKAF MEAIQAGADV SMIGQFGVGF YSAYLVAQNV MVTTKHHDDT
QLVWESAAGD SFTIREDKEG EKIPRGTRIS LLLKDDMLEY LEERKLKDLV KKHSEFIAYP
ITLQIDKTIE KEVEEEEEEE EEKKEEEKKE GEEEKKEGEE EKKEEEPKVE EEKKKEKKVR
RIKEVVKDFE QINKMKAIWM RKPEEITKEE YAAFYKSISN DWEDHLAVKH FFFEGSLEFR
AVLFAPRRAP FDMFETKKKN TNVKLYVRRV LTMESCEDLI PEYLSFIRGV VDPEDLPLNI
SRETLQQNKI MKVIKKNIVK KCIEMFLDIS ENKEDYAKFY EAFGKNLKLG IHEDADNHAK
LADLLRYCST KSPDEHISLK DYVSRMKPEQ KDIYYITGES KDAVKDSPFL ERLKRKDLEV
LFMVDPIDEY SVQQLKGYEG KKLLCVTKEG LEIDESDEEK RRREEMKAAN ENLCKVMKDI
LGEKVEKVCI STRVVDSPCI LVTNEYGWS
//
