ID A0A3B6LP12_WHEAT Unreviewed; 663 AA.
AC A0A3B6LP12;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EnsemblPlants:TraesCS5B02G258900.1};
GN ORFNames=CFC21_072142 {ECO:0000313|EMBL:KAF7066100.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5B02G258900.1};
RN [1] {ECO:0000313|EMBL:KAF7066100.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7066100.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5B02G258900.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5B02G258900.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS5B02G258900.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7066100.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7066100.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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; CM022224; KAF7066100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6LP12; -.
DR EnsemblPlants; TraesCS5B02G258900.1; TraesCS5B02G258900.1; TraesCS5B02G258900.
DR Gramene; TraesCAD_scaffold_116312_01G000100.1; TraesCAD_scaffold_116312_01G000100.1; TraesCAD_scaffold_116312_01G000100.
DR Gramene; TraesCLE_scaffold_029483_01G000300.1; TraesCLE_scaffold_029483_01G000300.1; TraesCLE_scaffold_029483_01G000300.
DR Gramene; TraesCS5B02G258900.1; TraesCS5B02G258900.1; TraesCS5B02G258900.
DR Gramene; TraesCS5B03G0672800.3; TraesCS5B03G0672800.3.CDS; TraesCS5B03G0672800.
DR Gramene; TraesPAR_scaffold_029344_01G000100.1; TraesPAR_scaffold_029344_01G000100.1; TraesPAR_scaffold_029344_01G000100.
DR Gramene; TraesROB_scaffold_086379_01G000100.1; TraesROB_scaffold_086379_01G000100.1; TraesROB_scaffold_086379_01G000100.
DR Gramene; TraesWEE_scaffold_025673_01G000300.1; TraesWEE_scaffold_025673_01G000300.1; TraesWEE_scaffold_025673_01G000300.
DR Proteomes; UP000019116; Chromosome 5B.
DR Proteomes; UP000815260; Chromosome 5B.
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; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR PANTHER; PTHR11528:SF99; HISTIDINE KINASE_HSP90-LIKE ATPASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 2.
DR PIRSF; PIRSF002583; Hsp90; 2.
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:UP000019116}.
FT DOMAIN 28..183
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 214..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 76169 MW; DA7B228C6F891785 CRC64;
MATETETFAF QAEINQLLSL IINTFYSNKE IFLRELISNS SDALDKIRFE SLTDKSKLDA
QPELFIHIIP DKATNTLTIV DSGIGMTKSD LVNNLGTIAR SGTKEFMEAL AAGADVSMIG
QFGVGFYSAY LVAERVVVTT KHNDDEQYVW ESQAGGSFTV TRDTSGEQLG RGTKMVLYLK
DDQMEYLEER RIKDLVKKHS EFISYPISLW TEKTTEKEIS DDEDEEEKKD TEEGKVEDVD
EEKEEKEKKK KKIKEVSHEW NLVNKQKPIW MRKPEEINKE EYAAFYKSLT NDWEEHLAVK
HFSVEGQLEF KAVLFVPKRA PFDLFDNKKK ANNIKLYVRR VFIMDNCEEL IPEYLSFVKG
IVDSEDLPLN ISRETLQQNK ILKVIRKNLV KKCIELFFEI AENKEDYNKF YEAFSKNLKL
GIHEDSQNRT KIAELLRYHS TKSGDELTSL KDYVTRMKEG QNEIYYITGE SKKGKKLVSA
TKEGLKLDES EDEKKKQEEL KEKFEGLCKV IKEVLGDKVE KVIVSDRVVD SPCCLVTGEY
GWTANMERIM KAQALRDSSM AGYMSSKKTM EINPENAIMD ELRKRADADK NDKSVKDLVM
LLFETSLLTS GFSLEDPNTF GTRIHRMLKL GLSIDEDDEA PENDTDMPPL EDDAGESKME
EVD
//
