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Database: UniProt
Entry: K2I0C9_ENTNP
LinkDB: K2I0C9_ENTNP
Original site: K2I0C9_ENTNP 
ID   K2I0C9_ENTNP            Unreviewed;       718 AA.
AC   K2I0C9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Heat shock protein 90, putative {ECO:0000313|EMBL:EKE42200.1};
GN   ORFNames=ENU1_029130 {ECO:0000313|EMBL:EKE42200.1};
OS   Entamoeba nuttalli (strain P19) (Amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=1076696 {ECO:0000313|EMBL:EKE42200.1, ECO:0000313|Proteomes:UP000006769};
RN   [1] {ECO:0000313|EMBL:EKE42200.1, ECO:0000313|Proteomes:UP000006769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P19 {ECO:0000313|EMBL:EKE42200.1,
RC   ECO:0000313|Proteomes:UP000006769};
RA   Hannick L., Karamycheva S., Lorenzi H., Caler E.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; JH925559; EKE42200.1; -; Genomic_DNA.
DR   RefSeq; XP_008855466.1; XM_008857244.1.
DR   AlphaFoldDB; K2I0C9; -.
DR   EnsemblProtists; EKE42200; EKE42200; ENU1_029130.
DR   GeneID; 20071640; -.
DR   VEuPathDB; AmoebaDB:ENU1_029130; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000006769; 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   Stress response {ECO:0000313|EMBL:EKE42200.1}.
FT   DOMAIN          37..193
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          226..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   718 AA;  82924 MW;  91877323DC695ADC CRC64;
     MGNRKDQSLE VEMTETYQFQ AEINQLLSLI INAFYSNKDI FLRELISNCS DALDKIRYQS
     LQDKSVLEAE PELVIRITAD KDNKQLIIED TGIGMTKADL INCLGTIARS GTKTFMSKII
     EGTADVSMIG QFGVGFYSSY LVAEKVTVIT KNNDDEQYIW ESSAGGEYTI TLDESGERLK
     RGTKIILKLK EDMQEYLETK KIQEIIKKHS EFIQYPIMLY VTKETEEEVT DDEAEEKKEE
     ETKEEDKKEE DVKIEDDKKE EEKPAKKTKK VKKVTHEWEQ VNKQKPIWTR NPSEITKEEY
     ASFYKTISND WEDHLAVKHF SVEGQIEFTA LLFVPQRAPF DMFETKKKPN NIKLYVRRVF
     IMDDCRELIP EWLGFIKGVV DSEDLPLNVS REMLQQNKIL KVIRKNLVKK CLELFVEISE
     NKEDFKKFYE AFGKNLKLGI HEDSTNRDKI AELLRFYSSK SGEDMTSFKD YIARMKENQK
     EIYFITGESK KAVETSPFVE GFVKKGIEVL YMTDPIDEYA MQQLKEFDGK KLVCITKDGI
     KVEETEEEKK EQEAKEKDNE ELSKVVKEIL GDKIEKVVIS NRLVNSPCAL VTGEYGWSAN
     MERIMKAQAL RDNSMSTYMV SKKTLEINPD HPIVQELRKR VHTDNSDKTV KDLVVLLFET
     ALLSSGFSLD EPAAFAGRIY RMVKLGLSLD DKEEEQATEA VPAVEETPIE DSKMEEVD
//
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