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HSP81_ORYSI
ID   HSP81_ORYSI             Reviewed;         699 AA.
AC   A2YWQ1; P33126; Q6ZK13;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Heat shock protein 81-1;
DE            Short=HSP81-1;
DE   AltName: Full=Heat shock protein 82;
GN   Name=HSP81-1; Synonyms=HSP82; ORFNames=OsI_028744;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Taichung native 1;
RX   PubMed=7764623; DOI=10.1007/bf00191607;
RA   van Breusegem F., de Keyser R., Garcia A., Claes B., Gielen J.,
RA   van Montagu M., Caplan A.;
RT   "Heat-inducible rice hsp82 and hsp70 are not always co-regulated.";
RL   Planta 193:57-66(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC       maintenance and proper regulation of specific target proteins involved
CC       for instance in cell cycle control and signal transduction. Undergoes a
CC       functional cycle that is linked to its ATPase activity. This cycle
CC       probably induces conformational changes in the client proteins, thereby
CC       causing their activation. Interacts dynamically with various co-
CC       chaperones that modulate its substrate recognition, ATPase cycle and
CC       chaperone function (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC       repeat-containing proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; Z11920; CAA77978.1; -; Genomic_DNA.
DR   EMBL; CM000133; EAZ07512.1; -; Genomic_DNA.
DR   PIR; S25541; S25541.
DR   AlphaFoldDB; A2YWQ1; -.
DR   SMR; A2YWQ1; -.
DR   STRING; 39946.A2YWQ1; -.
DR   iPTMnet; A2YWQ1; -.
DR   PRIDE; A2YWQ1; -.
DR   EnsemblPlants; BGIOSGA026730-TA; BGIOSGA026730-PA; BGIOSGA026730.
DR   Gramene; BGIOSGA026730-TA; BGIOSGA026730-PA; BGIOSGA026730.
DR   HOGENOM; CLU_006684_1_3_1; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000007015; Chromosome 8.
DR   GO; GO:0005737; C:cytoplasm; 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:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 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_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 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; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..699
FT                   /note="Heat shock protein 81-1"
FT                   /id="PRO_0000296246"
FT   REGION          215..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           695..699
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        232..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         373
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   699 AA;  80194 MW;  5381D14B572B3BCE CRC64;
     MASETETFAF QAEINQLLSL IINTFYSNKE IFLRELISNS SDALDKIRFE SLTDKSKLDA
     QPELFIHIVP DKASNTLSII DSGIGMTKSD LVNNLGTIAR SGTKEFMEAL AAGADVSMIG
     QFGVGFYSAY LVAERVVVTT KHNDDEQYVW ESQAGGSFTV TRDTSGEQLG RGTKITLYLK
     DDQLEYLEER RLKDLIKKHS EFISYPISLW TEKTTEKEIS DDEDEEEKKD AEEGKVEDVD
     EEKEEKEKKK KKIKEVSHEW SLVNKQKPIW MRKPEEITKE EYAAFYKSLT NDWEEHLAVK
     HFSVEGQLEF KAVLFVPKRA PFDLFDTRKK LNNIKLYVRR VFIMDNCEEL IPEWLSFVKG
     IVDSEDLPLN ISREMLQQNK ILKVIRKNLV KKCVELFFEI AENKEDYNKF YEAFSKNLKL
     GIHEDSTNRN KIAELLRYHS TKSGDELTSL KDYVTRMKEG QNDIYYITGE SKKAVENSPF
     LEKLKKKGYE VLYMVDAIDE YAVGQLKEFE GKKLVSATKE GLKLDESEDE KKRKEELKEK
     FEGLCKVIKE VLGDKVEKVV VSDRVVDSPC CLVTGEYGWT ANMERIMKAQ ALRDSSMAGY
     MSSKKTMEIN PENAIMEELR KRADADKNDK SVKDLVLLLF ETALLTSGFS LDDPNTFGSR
     IHRMLKLGLS IDEDETAEAD TDMPPLEDDA GESKMEEVD
 
 
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