ID A1DZR4_9ACAR Unreviewed; 180 AA.
AC A1DZR4;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Heat shock protein 82 {ECO:0000313|EMBL:ABL10404.1};
DE Flags: Fragment;
GN Name=hsp82 {ECO:0000313|EMBL:ABL10404.1};
OS Nothrus silvestris.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Oribatida; Desmonomata; Crotonioidea;
OC Nothridae; Nothrus.
OX NCBI_TaxID=66602 {ECO:0000313|EMBL:ABL10404.1};
RN [1] {ECO:0000313|EMBL:ABL10404.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17438282; DOI=10.1073/pnas.0700034104;
RA Domes K., Norton R.A., Maraun M., Scheu S.;
RT "Reevolution of sexuality breaks Dollo's law.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7139-7144(2007).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; EF081333; ABL10404.1; -; Genomic_DNA.
DR AlphaFoldDB; A1DZR4; -.
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 Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF00183; HSP90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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:ABL10404.1}.
FT REGION 85..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL10404.1"
FT NON_TER 180
FT /evidence="ECO:0000313|EMBL:ABL10404.1"
SQ SEQUENCE 180 AA; 21153 MW; 172F94B06D161D15 CRC64;
SAYLIADRVT VTSKHNDDEQ YVWESSAGGS FTIRTDSAEP LGRGTKIVLN LKEDQLEYAE
EKRIKDIVKK HSQFIGYPIK LLVQKEREKE VSDDEEDKDE ENKDKTESEK KSDEDITEDK
KEESDEPKIE DVEDSEDKEK DKKKKKKIKE KYVEDEELNK TKPIWMRNPD DITQEEYGDF
//