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Database: UniProt
Entry: A1DZR4_9ACAR
LinkDB: A1DZR4_9ACAR
Original site: A1DZR4_9ACAR 
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
//
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