ID A0A0L1L0Q5_9EUGL Unreviewed; 702 AA.
AC A0A0L1L0Q5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Heat shock protein 85 {ECO:0000313|EMBL:KNH09706.1};
GN ORFNames=XU18_0391 {ECO:0000313|EMBL:KNH09706.1};
OS Perkinsela sp. CCAP 1560/4.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Prokinetoplastina;
OC Ichthyobodonidae; Perkinsela.
OX NCBI_TaxID=1314962 {ECO:0000313|EMBL:KNH09706.1, ECO:0000313|Proteomes:UP000036983};
RN [1] {ECO:0000313|EMBL:KNH09706.1, ECO:0000313|Proteomes:UP000036983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1560/4 {ECO:0000313|EMBL:KNH09706.1};
RA Tanifuji G., David V., Flegontov P., Gerasimov E., Hashimi H.,
RA Logacheva M., Maruyama S., Onodera N., Gray M., Archibald J., Curtis B.,
RA Cenci U., Lukes J.;
RT "Draft genomes of Paramoeba pemaquidensis and its kinetoplastid
RT endosymbiont Perkinsela sp. CCAP 1560/4.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle that is linked to its ATPase activity. This cycle
CC probably induces conformational changes in the client proteins, thereby
CC causing their activation. Interacts dynamically with various co-
CC chaperones that modulate its substrate recognition, ATPase cycle and
CC chaperone function. {ECO:0000256|ARBA:ARBA00037441}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNH09706.1}.
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DR EMBL; LFNC01000001; KNH09706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L1L0Q5; -.
DR EnsemblProtists; KNH09706; KNH09706; XU18_0391.
DR OrthoDB; 167727at2759; -.
DR Proteomes; UP000036983; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
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.
DR PROSITE; PS00298; HSP90; 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 Reference proteome {ECO:0000313|Proteomes:UP000036983};
KW Stress response {ECO:0000313|EMBL:KNH09706.1}.
FT DOMAIN 25..179
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 210..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 80131 MW; BCBA4C2B8CA9B904 CRC64;
MTETFAFQAE INQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRHQSLT DPSALAADST
LHIQIIANKA EKTLSIIDTG VGMTKADMVN NLGTIARSGT KSFMEALESG ADLSMIGQFG
VGFYSAYLVA DRVRVTSKHN DDEAHVWESA AGGTFTVTTC PETSIKRGTI ITLFLKEDQL
EYLEERKIKD LVKKHSEFIA YDIELQVERT TEREVTDDEA DEEEKAAESE EKPADDDAKV
EEATEEKKKK TKKVKDVSLE FDVLNKSKPI WTRDPKEVKP EEYAAFYKTI SNDWEDHLAV
KHFSVEGQLE FRAVLFAPKR APFDMFEPSK KRNNIKLYVR RVFIMDNCEE ICPEWLAFLR
GVVDSEDLPL NISRESLQQN KILKVIKKNI VKKAIELFEE IAGNADDYKK FYEQFGKNLK
LGIHEDSANR TKLADLLRYY STKSTDEPTS LKDYVTRMKD GQKTIYYISG DSQKKLESSP
FLEEARRRDQ EVLFMVDPID EYVMQQLKEF EDKKFVCLTK EGLTFEETEE EKKKREEETA
SFEQLCKTIK EVLGDKVEKV VLTSRLATSP CILVTSEHGW SAHMEQIMKH QALRDSSMSS
YMVSKKTMEI NPKHSIVKEL RAKADADQND KTVKDLVMLL FDTALLTSGF SLEDPSGYAN
RIHRMIKLGL SLDDAEEEAP AAEKVEEITA EDHGDSEMQE VD
//
