HSP90_ASPFU
ID HSP90_ASPFU Reviewed; 706 AA.
AC P40292; Q4WET9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Heat shock protein 90;
DE AltName: Full=65 kDa IgE-binding protein;
DE AltName: Full=Heat shock protein hsp1;
DE AltName: Allergen=Asp f 12;
GN Name=hsp90; Synonyms=hsp1; ORFNames=AFUA_5G04170;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 266-706.
RA Kurup V.P., Banerjee B.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 430-549.
RC STRAIN=ATCC 42202 / AF-102 / Ag 507;
RX PubMed=8491935; DOI=10.1016/0091-6749(93)90215-2;
RA Kumar A., Reddy L.V., Sochanik A., Kurup V.P.;
RT "Isolation and characterization of a recombinant heat shock protein of
RT Aspergillus fumigatus.";
RL J. Allergy Clin. Immunol. 91:1024-1030(1993).
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:0000250}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AAHF01000011; EAL85888.1; -; Genomic_DNA.
DR EMBL; U92465; AAB51544.1; -; mRNA.
DR RefSeq; XP_747926.1; XM_742833.1.
DR AlphaFoldDB; P40292; -.
DR SMR; P40292; -.
DR STRING; 746128.CADAFUBP00005158; -.
DR Allergome; 3110; Asp f 12.0101.
DR Allergome; 65; Asp f 12.
DR SwissPalm; P40292; -.
DR PRIDE; P40292; -.
DR EnsemblFungi; EAL85888; EAL85888; AFUA_5G04170.
DR GeneID; 3505604; -.
DR KEGG; afm:AFUA_5G04170; -.
DR VEuPathDB; FungiDB:Afu5g04170; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P40292; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 924636at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0030428; C:cell septum; IDA:AspGD.
DR GO; GO:0005829; C:cytosol; IDA:AspGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:AspGD.
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:0140453; C:protein aggregate center; IEA:EnsemblFungi.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0010619; P:adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IEA:EnsemblFungi.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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 1: Evidence at protein level;
KW Allergen; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..706
FT /note="Heat shock protein 90"
FT /id="PRO_0000062960"
FT REGION 214..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 702..706
FT /note="TPR repeat-binding"
FT COMPBIAS 217..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 706 AA; 80640 MW; 8C6389FC933934D8 CRC64;
MSSETFEFQA EISQLLSLII NTVYSNKEIF LRELISNASD ALDKIRYQSL SDPTKLDTGK
DLRIDIIPDK ENKTLTIRDT GIGMTKADLI NNLGTIARSG TKQFMEALSA GADISMIGQF
GVGFYSAYLV ADRVTVVSKN NDDEQYIWES AAGGTFTLTQ DTEGEQLGRG TKIILHLKDE
QTDYLNESRI KEVVRKHSEF ISYPIYLHVL KETEKEVPDE EAEETKEEED EEKKAKIEEV
DDEEEEEKKK KKKTKTVKES KIEEEELNKT KPIWTRNPAD ITQEEYASFY KSLSNDWEDH
LAVKHFSVEG QLEFRAILYV PKRAPFDLFE TKKTKNNIKL YVRRVFITDD ATDLIPEWLG
FIKGVVDSED LPLNLSRETL QQNKIMKVIK KNIVKKTLEL FNEIAEDREQ FDKFYSAFSK
NIKLGIHEDA QNRQTLAKLL RYQSTKSGDE ATSLADYVTR MPEHQKQIYY ITGESIKAVA
KSPFLDSLKQ KNFEVLFLVD PIDEYAFTQL KEFDGKKLVD ITKDFELEET EEEKAEREKE
EKEYENLAKS LKNILGDKVE KVVVSHKLVG SPCAIRTGQF GWSANMERIM KAQALRDTSM
SSYMSSKKTF EISPKSSIIK ELKKKVEADG ENDRTVKSIT QLLFETSLLV SGFTIEEPAS
FAERIHKLVS LGLNIDEEAE TTEEKATEEA APAEATTGES AMEEVD
