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Database: UniProt
Entry: A0A078FF63_BRANA
LinkDB: A0A078FF63_BRANA
Original site: A0A078FF63_BRANA 
ID   A0A078FF63_BRANA        Unreviewed;       537 AA.
AC   A0A078FF63;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=BnaC03g13470D protein {ECO:0000313|EMBL:CDY11921.1};
GN   Name=BnaC03g13470D {ECO:0000313|EMBL:CDY11921.1};
GN   ORFNames=GSBRNA2T00060765001 {ECO:0000313|EMBL:CDY11921.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY11921.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY11921.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; LK032015; CDY11921.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078FF63; -.
DR   STRING; 3708.A0A078FF63; -.
DR   PaxDb; 3708-A0A078FF63; -.
DR   EnsemblPlants; CDY11921; CDY11921; GSBRNA2T00060765001.
DR   Gramene; CDY11921; CDY11921; GSBRNA2T00060765001.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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   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:SF133; HEAT SHOCK PROTEIN 90-2-RELATED; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 3.
DR   PIRSF; PIRSF002583; Hsp90; 3.
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:UP000028999}.
FT   DOMAIN          27..165
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          158..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..203
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  60990 MW;  C4392D02A26B478C CRC64;
     MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES LTDKSKLDGQ
     PELFIHIIPD KTNNTLTIID SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ
     FGVGFYSAYL VADKVIVTTK HNDDEQYVWE SQAGGSFTVT RDTSGENGPS PQGGPVGTIE
     KEISDDEDEE EKKDEEGKVE EVDEEKEKEE KKKKKIKEVS HEWDLVNKQK PIWMRKPEEI
     TKEEYAAFYK SLSNDWEEHL AVKHFSVEGQ LEFKAVLFVP KRAPFDLFDT KKKPNNIKLY
     VRRVFIMDNC EDIIPEWLGF QNKILKVIRK NLVKKCLELF FEVAENKEDY NKTKIAELLR
     QEDIFYITGE SKKAVENSPF LEKLKKKGFE VLYMVDAIDE YAIGQLKEFE GKKLVSATKE
     ELKEKFEGLC KVIKDVLGDK VEKVIVSDRV VDSPCCLVTG EYGWTANMER IMKAQALRDS
     SMAGYILDEP NTFGSRIHRM LKLGLSIDED DAVEADAEMP PLEDDADAEG SKMEEVD
//
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