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Database: UniProt
Entry: F4Y5A8_TRIUA
LinkDB: F4Y5A8_TRIUA
Original site: F4Y5A8_TRIUA 
ID   F4Y5A8_TRIUA            Unreviewed;       700 AA.
AC   F4Y5A8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   08-NOV-2023, entry version 53.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ADF31773.1};
GN   Name=Hsp90.2-A1 {ECO:0000313|EMBL:ADF31773.1};
OS   Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4572 {ECO:0000313|EMBL:ADF31773.1};
RN   [1] {ECO:0000313|EMBL:ADF31773.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang G., Zhou H., Wang X., Ling H., Wang D., Zhang X.;
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADF31773.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21488877; DOI=10.1111/j.1469-8137.2011.03715.x;
RA   Wang G.F., Wei X., Fan R., Zhou H., Wang X., Yu C., Dong L., Dong Z.,
RA   Wang X., Kang Z., Ling H., Shen Q.H., Wang D., Zhang X.;
RT   "Molecular analysis of common wheat genes encoding three types of cytosolic
RT   heat shock protein 90 (Hsp90): functional involvement of cytosolic Hsp90s
RT   in the control of wheat seedling growth and disease resistance.";
RL   New Phytol. 191:418-431(2011).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; GQ240791; ADF31773.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4Y5A8; -.
DR   ExpressionAtlas; F4Y5A8; differential.
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:SF137; HEAT SHOCK PROTEIN 81-3; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF02518; HATPase_c; 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   Stress response {ECO:0000313|EMBL:ADF31773.1}.
FT   DOMAIN          28..183
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          215..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..700
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   700 AA;  80391 MW;  944F9C9E507C3198 CRC64;
     MASETETFAF QAEINQLLSL IINTFYSNKE IFLRELISNA SDALDKIRFE SLTDKSKLDA
     PPELFIHIIP DKATNTLTLI DSGIGMTKSD LVNNLGTIAR SGTKDFMEAL AAGADVSMIG
     QFGVGFYSAY LVAERVVVTS KHNDDEQYVW ESQAGGSFTV TRDTTGEPLG RGTKITLYLK
     DDQLEYLEER RLKDLVKKHS EFISYPISLW TEKTTEKEIS DDEDEDEKKD TEEGKVEEID
     EEKEEKEKKK KKIKEVSHEW NLINKQKPIW MRKPEEITKD EYAAFYKSLT NDWEEHLAVK
     HFSVEGQLEF KAVLFVPKRA PFDLFDTRKK LNNIKLYVRR VFIMDNCEEL IPEWLSFVKG
     IVDSEDLPLN ISRETLQQNK ILKVIRKNLV KKCIELFFEI AENKEDYNKF YEAFSKNLKL
     GVHEDSTNRT KLAELLRYHS TKSGDELTSL KDYVTRMKEG QNDIYYITGE SKKAVENSPF
     LEKLKKKGYE VLYMVDAIDE YSIGQLKEFE GKKLVSATKE GLKLDDSEEE KKRKEELKEK
     FEGLCKVIKE VLGDRVEKVI VSDRVVDSPC CLVTGEYGWT ANMERIMKAQ ALRDTSMGGY
     MSSKKTMEIN PENAIMEELR KRADADKNDK SVKDLVMLLF ETSLLTSGFS LDDPNTFGTR
     IHRMLKLGLS IDEDEEAAEA DTDMPPLEED AGESKMEEVD
//
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