ID A1C299_9EUKA Unreviewed; 568 AA.
AC A1C299;
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:ABL11329.1};
DE Flags: Fragment;
GN Name=hsp90 {ECO:0000313|EMBL:ABL11329.1};
OS uncultured Oxymonadida sp.
OC Eukaryota; Metamonada; Preaxostyla; Oxymonadida; environmental samples.
OX NCBI_TaxID=413579 {ECO:0000313|EMBL:ABL11329.1};
RN [1] {ECO:0000313|EMBL:ABL11329.1}
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}.
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DR EMBL; DQ925180; ABL11329.1; -; Genomic_DNA.
DR AlphaFoldDB; A1C299; -.
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:ABL11329.1}.
FT DOMAIN 2..157
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 192..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL11329.1"
FT NON_TER 568
FT /evidence="ECO:0000313|EMBL:ABL11329.1"
SQ SEQUENCE 568 AA; 66247 MW; D406A8E56CBEF7C5 CRC64;
SNKDIFLREL ISNASDALDK IRYRSLTDKA LLEEEPRFEI RLIPDKVNKI LHICDTGVGM
TETELVNNLG TIASSGTKAF MEAIQAGADV SMIGQFGVGF YSAYLVAQNV MVTTKHHDDT
QLVWESAAGD SFTIREDKEG EKIPRGTRIS LLLKDDMLEY LEERKLKDLV KKHSEFIAYP
ITLQIDKTIE KEVEEEEEEE EKKEEEKKEG EEEKKEGEEE KKEEEPKVEE EKKKEKKVRR
IKEVVKDFEQ INKMKAIWMR KPEEITKEEY AAFYKSISND WEDHLAVKHF FFEGSLEFRA
VLFAPRRAPF DMFETKKKNT NVKLYVRRVL IMENCEDLIP EYLSFIRGVV DPEDLPLNIS
RETLQQNKIM KVIKKNIVKK CIEMFLDISE SKEDYAKFYE AFGKNLKLGI HEDADNRAKL
ADLLRYCSTK SPDEHISLKD YVSRMKPEQK DIYYITGESK DAVKDSPFLE RLKRKDLEVL
FMVDPIDEYS VQQLKEYEGK KLLCVTKEGL EIDESDEEKR RREEMKAANE NLCKVMKDIL
GEKVEKVCIS TRVVDSPCIL VTNEYGWS
//
