ID A0A2I0B463_9ASPA Unreviewed; 822 AA.
AC A0A2I0B463;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Endoplasmin like {ECO:0000313|EMBL:PKA62580.1};
GN Name=HSP90 {ECO:0000313|EMBL:PKA62580.1};
GN ORFNames=AXF42_Ash012166 {ECO:0000313|EMBL:PKA62580.1};
OS Apostasia shenzhenica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Apostasioideae; Apostasia.
OX NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA62580.1, ECO:0000313|Proteomes:UP000236161};
RN [1] {ECO:0000313|EMBL:PKA62580.1, ECO:0000313|Proteomes:UP000236161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC TISSUE=Stem {ECO:0000313|EMBL:PKA62580.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; KZ451916; PKA62580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0B463; -.
DR STRING; 1088818.A0A2I0B463; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000236161; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; 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:SF97; ENDOPLASMIN; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..822
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014180541"
FT DOMAIN 102..259
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 49..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 94324 MW; ECA27CD0A9E40E23 CRC64;
MRKWAIPSAL LLLLFLSAIP DHDRKLQANA DSSGDSDDLV DPPKIEEKLG AVPSGVSTDS
DVAKREAESM SRKTLRSNAE KFEFQAEVSR LMDIIINSLY SNKDIFLREL ISNGSDALDK
IRFLSLTDKE VLGEGENTKL EILIKLDKEK KVLSIRDRGI GMTKEDLIKN LGTIAKSGTS
AFVEKMQASG DLSLIGQFGV GFYSVYLVSD YVEVISKHND DKQYVWESKA DGSFGISEDT
WNEPLGRGTE IRLHLRDEAK EYLDETKLKE LVKKYSEFIN FPIYLWASKE IDVEVPSDEE
ESGEEDSSET STSEEETEED EAEKKPKKKT VKETTYEWEL LNDMKAIWLR NPKEVTEEEY
NKFYQSISKD ITDEKPLGWT HFNAEGDVEF KALLFVPPKA PHDLYESYYN TKKSNLKLYV
RRVFISDEFD ELLPKYLNFL KGLVDSDTLP LNVSREMLQQ HSSLKTIKKK LIRKALDMIR
RIADEDPDEY TNKNKTDAEK VSENEDKKGQ YTKFWNEFGK SIKLGIIEDA QNRNRLAKLL
RFESTKSEGK LTSLDEYISR MKSGQKDIFY ITGTNKEQLE KSPFLERLTK KNYEVIFFTD
PVDEYLMQYL MDYEDKHFQN VSKEGLNLGK ESKNKDLKES FKELTKWWKN ALSSENVDSV
KISNRLDNTP CVVVTSKYGW SANMEKIMQA QTLSDAAKQA YMRGKRVLEI NPRHPIIKEL
RERVATDAED ESLKQTARLV YQTALMESGF LLSDPKDFAS SIYSSVKTSL NISPDVAVEE
EEEAEETEAE DSKESSSSSK EAEADDAIKE EEAEYTYEKD EL
//
