ID A0A078FDC9_BRANA Unreviewed; 871 AA.
AC A0A078FDC9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=(rape) hypothetical protein {ECO:0000313|EMBL:CAF2131105.1};
DE SubName: Full=BnaA03g46510D protein {ECO:0000313|EMBL:CDY10992.1};
GN Name=BnaA03g46510D {ECO:0000313|EMBL:CDY10992.1};
GN ORFNames=DARMORV10_A03P55100.1 {ECO:0000313|EMBL:CAF2131105.1},
GN GSBRNA2T00048937001 {ECO:0000313|EMBL:CDY10992.1};
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:CDY10992.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY10992.1, 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).
RN [2] {ECO:0000313|EMBL:CDY10992.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAF2131105.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope - CEA;
RA William W.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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; HG994357; CAF2131105.1; -; Genomic_DNA.
DR EMBL; LK032008; CDY10992.1; -; Genomic_DNA.
DR STRING; 3708.A0A078FDC9; -.
DR PaxDb; 3708-A0A078FDC9; -.
DR EnsemblPlants; CDY10992; CDY10992; GSBRNA2T00048937001.
DR Gramene; CDY10992; CDY10992; GSBRNA2T00048937001.
DR OMA; WFEAFNI; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006457; P:protein folding; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..871
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040561353"
FT TRANSMEM 822..849
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..256
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 29..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..315
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 100514 MW; 2195F7083A7AA23D CRC64;
MRKRTLVSVL FLFSLLFLLP DQGRKLHANA EDSSDEVTDP PKVEEKLGGH SGLSTDSDVV
HRESESISKK SLRSNAEKFE FQAEVSRLMD IIINSLYSNK DIFLRELISN ASDALDKIRF
LALTDKDVLG EGDTAKLEIQ IKLDKAKKII SIRDRGIGMT KEDLIKNLGT IAKSGTSAFV
EKMQSSGDLN LIGQFGVGFY STYLVADYIE VISKHNDDIQ HVWESKADGK FAVSEDTWNE
PLGRGTEIRL HLRDEAGEYL EESKLKRYSE FINFPIHLWA SKEVETEVPV EEDESTEEET
ETPSTEEEKE EDAEDEDSEK KQKTKKVKET VYEWELLNDV KAIWLRSPKE VTEEEYTKFY
HSLSKDFSEE KPMAWSHFNA EGDVEFKAVL YVPPKAPHDL YESYYNSNKA NLKLYVRRVF
ISDEFDELLP KYLSFLKGLV DSDTLPLNVS REMLQQHSSL KTIKKKLIRK ALDMIRKLAE
EDPDEVHDDD KKDVEKSGEN DEKKGQYSKF WNEFGKSIKL GIIEDASNRN RLAKLLRFET
TKSDGKLTSL DQYIKRMKKG QKDVFYITGS SKEQLEKSPF LERLIKKGYE VIFFTDPVDE
YLMQYLMDYE DKKFQNVSKE GLKVGKDSKV KELKEAFKEL TKWWKESLAS ENVDDVKISN
RLADTPCVVV ASKFGWSANM ERIMQSQTLS DANKQAYMRG KRVLEINPRH PIIKELKERV
ASDPEDESVK ETAQLMYQTA LIESGFVLND PKDFAGRIYN SVKSSLKISP DAVAEEEVEA
EETETSEEAT EAKSDDLAGG LNIEAEQVEE RRQPRMNCRF HLVMFFLIYV FLYSLVKSRI
LVFFTIWFLM DYVKATQHVF WFEAFNILLK Q
//
