HSP82_ASHGO
ID HSP82_ASHGO Reviewed; 704 AA.
AC Q8J2M3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Heat shock protein HSP82;
GN Name=HSP82; OrderedLocusNames=AFL148C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wendland J.W., Dietrich F.S., Gaffney T.D., Philippsen P.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AF431814; AAN61917.1; -; Genomic_DNA.
DR EMBL; AE016819; AAS53226.1; -; Genomic_DNA.
DR RefSeq; NP_985402.1; NM_210756.1.
DR AlphaFoldDB; Q8J2M3; -.
DR SMR; Q8J2M3; -.
DR STRING; 33169.AAS53226; -.
DR PRIDE; Q8J2M3; -.
DR EnsemblFungi; AAS53226; AAS53226; AGOS_AFL148C.
DR GeneID; 4621628; -.
DR KEGG; ago:AGOS_AFL148C; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; Q8J2M3; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000000591; Chromosome VI.
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: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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..704
FT /note="Heat shock protein HSP82"
FT /id="PRO_0000062956"
FT REGION 219..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 700..704
FT /note="TPR repeat-binding"
FT COMPBIAS 219..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 704 AA; 80696 MW; 65D575DD1B48A9B5 CRC64;
MSSQETYEFQ AEITQLMSLI INTVYSNKEI FLRELISNAS DALDKIRYQS LSDPKVLESD
PELFIRLTPK PEEKVLEIRD SGIGMTKAEL INNLGTIAKS GTKAFMEALS AGADVSMIGQ
FGVGFYSLFL VADRVQVISK HNDDEQYIWE SNAGGSFTVT LDEVNERIGR GTILRLFLKE
DQLEYLEEKR IKEVVKRHSE FVAYPIQLLV TKEVEKEVPV EEEEKKEETE DDKKPKLEEV
DEEEEDKEKS KTKKVKENVK ELEELNKTKP LWTRNPSEVT QEEYNAFYKS ISNDWEDPLA
VKHFSVEGQL EFRAILFIPK RAPFDLFESK KKKNNIKLYV RRVFITDEAE ELIPEWLSFV
KGVVDSEDLP LNLSREMLQQ NKIMKVIKKN IVKKLIEAFN EIAEDSEQFE KFYSAFAKNI
KLGIHEDSQN RASLAKLLRY NSTKSVDEQT SLADYVTRMP EHQKNVYFIT GESIKAVEKS
PFLDALKAKN FEVLFLVDPI DEYAFQQLKE FEGKQLVDIT KDFELEESEE EKKQREEEIK
EFEPLTAALK EVLGDQVEKV VVSYKLIDAP AAIRTGQFGW SANMERIMKA QALRDSTMSS
YMASKKIFEI SPKSAIIKEL KKRVEDNGAQ DRTVKDLTSL LYETALLTSG FTLEEPASFA
TRINRLISLG LNIDEEESTE TAAETATEAP VEEVAPETAM EEVD
