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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
 
 
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