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Database: UniProt
Entry: E5DGQ2_9DINO
LinkDB: E5DGQ2_9DINO
Original site: E5DGQ2_9DINO 
ID   E5DGQ2_9DINO            Unreviewed;       567 AA.
AC   E5DGQ2;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ADP65788.1};
DE   Flags: Fragment;
OS   Gymnodinium fuscum.
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Gymnodiniales; Gymnodiniaceae;
OC   Gymnodinium.
OX   NCBI_TaxID=66466 {ECO:0000313|EMBL:ADP65788.1};
RN   [1] {ECO:0000313|EMBL:ADP65788.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20949037; DOI=10.1371/journal.pone.0013220;
RA   Hoppenrath M., Leander B.S.;
RT   "Dinoflagellate phylogeny as inferred from heat shock protein 90 and
RT   ribosomal gene sequences.";
RL   PLoS ONE 5:E13220-E13220(2010).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; GU295194; ADP65788.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5DGQ2; -.
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   HAMAP; MF_00505; HSP90; 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:ADP65788.1}.
FT   REGION          188..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADP65788.1"
FT   NON_TER         567
FT                   /evidence="ECO:0000313|EMBL:ADP65788.1"
SQ   SEQUENCE   567 AA;  65431 MW;  984820422BC40C88 CRC64;
     VFLRELISNA SDALDKIRYE SITDPEKIEA QPNFFIKIIP DKTNSTLTIE DSGIGMTKNE
     LVNNLGTIAK SGTKAFMEAM AAGGDISMIG QFGVGFYSAY LVSDKVRVVS KNNDDEQYIW
     ESAAGGSFTV QKDTELVHGE VKRGTKVICY LKEDQSEFLE ERRLKDLVKK HSEFIGFPIE
     LYVEKSKEKE VTDSEDEEEA KKEEGKEGDE PKIEEVDEEK EKEEKKKKTK KVKEVSHEWE
     QLNKNKPLWM RKSEDVTNEE YASFYKSLSN DWEDHLAVKH FSVEGQLEFR ALLFVPRRAP
     FDLFETKKKR NNIKLYVRRV FIMDDCDELM PDWLNMVKGV VDSEDLPLNI SRETLQQNKI
     LRVIKKNLVK KCLEMFAEIA ERKDDYKKFY EQFGKCLKLG VHEDSTNRAK VAELMRYQTS
     KSGDEQISLK EYIDRMKEGQ SDIYYITGES IAAVSCSPFL ETLRKKGLEV LYMVDPIDEY
     AVQQLKEFDG KKLKSVTKEG LDVDDEDEKK KMEELKAEFE PLTKLMKEVL GDKVEKVVIS
     SRMADSPCVL TTSEYGWSAN MERIMKA
//
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