ID A0A059BX04_EUCGR Unreviewed; 619 AA.
AC A0A059BX04;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EUGRSUZ_F03673 {ECO:0000313|EMBL:KCW70451.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW70451.1};
RN [1] {ECO:0000313|EMBL:KCW70451.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW70451.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; KK198758; KCW70451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059BX04; -.
DR EnsemblPlants; KCW70451; KCW70451; EUGRSUZ_F03673.
DR Gramene; KCW70451; KCW70451; EUGRSUZ_F03673.
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; 3.30.230.80; -; 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:SF138; HEAT SHOCK COGNATE PROTEIN 80; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT REGION 131..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..158
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..619
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 71129 MW; 8CB3CC7B3E304097 CRC64;
MTKADLVNNL GTIARSGTKE FMEALAAGAD VSMIGQFGVG FYSAYLVAEK VVVTTKHYDD
EQYVWESQAG GSFTVTRDTS GEILGRGTKI TLLLKEDQLE YLEERRLKDL IKKHSEFISY
PISLWVEKTT EKEISDDEDE EDKKEEKEDE EGKVEDVDEE KDTEEKKKKK IKEVSHEWSL
VNKQKPIWMR KPEEITKEEY AAFYKSLTND WEEHLAVKHF SVEGQLEFKA ILYAPKRAPF
DLFDTRKKPN NIKLYVRRVF IMDNCEELMP EYLGFVKGIV DSEDLPLNIS REMLQQNKIL
KVIRKNLVKK CIELFFEIAE NKEDYNKFYE AFSKNLKLGI HEDSQNKTKL AELLRYHSTK
SGEELTSLKD YVTRMKEGQQ DIYYITGESK KAVENSPFLE KLRKKGYEVL YMVDAIDEYA
VGQLKEYEGK KLVSATKEGL KLDESEDEKK KSEELKAKFE GLCKVVKDVL GDKVEKVVVS
DRVVDSPCCL VTGEYGWTAN MERIMKAQAL RDNSMAGYMS SKKTMEINPE NPIMEELRKR
ADADKNDKSV KDLVLLLFET ALLTSGFSLD EPNTFGNRIH RMLKLGLSID EDAPDGDADM
PPLEDAEVEA EGSKMEEVD
//
