HSP85_TRYCR
ID HSP85_TRYCR Reviewed; 704 AA.
AC P06660;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Heat shock-like 85 kDa protein;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Peru;
RX PubMed=3550435; DOI=10.1128/mcb.7.3.1271-1275.1987;
RA Dragon E.A., Sias S.R., Kato E.A., Gabe J.D.;
RT "The genome of Trypanosoma cruzi contains a constitutively expressed,
RT tandemly arranged multicopy gene homologous to a major heat shock
RT protein.";
RL Mol. Cell. Biol. 7:1271-1275(1987).
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.
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; M15346; AAA30202.1; -; Genomic_DNA.
DR PIR; A26125; A26125.
DR AlphaFoldDB; P06660; -.
DR SMR; P06660; -.
DR PRIDE; P06660; -.
DR VEuPathDB; TriTrypDB:BCY84_06243; -.
DR VEuPathDB; TriTrypDB:BCY84_06244; -.
DR VEuPathDB; TriTrypDB:BCY84_06245; -.
DR VEuPathDB; TriTrypDB:BCY84_06246; -.
DR VEuPathDB; TriTrypDB:BCY84_06247; -.
DR VEuPathDB; TriTrypDB:BCY84_06248; -.
DR VEuPathDB; TriTrypDB:BCY84_10963; -.
DR VEuPathDB; TriTrypDB:BCY84_10964; -.
DR VEuPathDB; TriTrypDB:BCY84_10970; -.
DR VEuPathDB; TriTrypDB:BCY84_10971; -.
DR VEuPathDB; TriTrypDB:BCY84_10972; -.
DR VEuPathDB; TriTrypDB:BCY84_10973; -.
DR VEuPathDB; TriTrypDB:BCY84_10974; -.
DR VEuPathDB; TriTrypDB:BCY84_10978; -.
DR VEuPathDB; TriTrypDB:BCY84_10979; -.
DR VEuPathDB; TriTrypDB:BCY84_10980; -.
DR VEuPathDB; TriTrypDB:BCY84_10981; -.
DR VEuPathDB; TriTrypDB:BCY84_10982; -.
DR VEuPathDB; TriTrypDB:BCY84_10986; -.
DR VEuPathDB; TriTrypDB:BCY84_10987; -.
DR VEuPathDB; TriTrypDB:BCY84_10988; -.
DR VEuPathDB; TriTrypDB:BCY84_10989; -.
DR VEuPathDB; TriTrypDB:BCY84_10990; -.
DR VEuPathDB; TriTrypDB:C3747_60g185; -.
DR VEuPathDB; TriTrypDB:C4B63_113g25; -.
DR VEuPathDB; TriTrypDB:C4B63_113g29; -.
DR VEuPathDB; TriTrypDB:C4B63_113g30; -.
DR VEuPathDB; TriTrypDB:C4B63_84g87; -.
DR VEuPathDB; TriTrypDB:C4B63_84g88; -.
DR VEuPathDB; TriTrypDB:C4B63_84g89; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_3581; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0002250; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0002260; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0002270; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0002280; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0015160; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0015170; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0064950; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0064960; -.
DR VEuPathDB; TriTrypDB:TcCL_NonESM02852; -.
DR VEuPathDB; TriTrypDB:TcCLB.507713.30; -.
DR VEuPathDB; TriTrypDB:TcCLB.509105.140; -.
DR VEuPathDB; TriTrypDB:TCDM_06775; -.
DR VEuPathDB; TriTrypDB:TcG_07416; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_008621; -.
DR VEuPathDB; TriTrypDB:TcYC6_0072610; -.
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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT CHAIN 1..704
FT /note="Heat shock-like 85 kDa protein"
FT /id="PRO_0000062945"
FT REGION 212..251
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 BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 123
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; 80758 MW; EC39D45576FBFA67 CRC64;
MTETFAFQAE INQLMSLIIN TFYSNKEIFL RELISNSSDA CDKIRYQSLT NQAVLGDESH
LRIRVVPDKA NKTLTVEDTG IGMTKAELVN NLGTIARSGT KAFMEALEAG GDMSMIGQFG
VGFYSAYLVA DRVTVVSKNN DDEAYTWESS AGGTFTVTPT PDCDLKRGTR IVLHLKEDQQ
EYLEERRLKD LIKKHSEFIG YDIELMVEKA TEKEVTDEDE DEAAATKNEE GEEPKVEEVK
DDAEEGEKKK KTKKVKEVTQ EFVVQNKHKP LWTRDPKDVT KEEYAAFYKA ISNDWEEPLS
TKHFSVEGQL EFRAILFVPK RAPFDMFEPS KKRNNIKLYV RRVFIMDNCE DLCPEWLAFV
RGVVDSEDLP LNISRENLQQ NKILKVIRKN IVKKALELFE EIAENKEDYK KFYEQFGKNV
KLGIHEDSAN RKKLMELLRF HSSESGEDMT TLKDYVTRMK EGQKCIYYVT GDSKKKLETS
PFIEQARRRG FEVLFMTEPI DEYVMQQVKD FEDKKFACLT KEGVHFEETE EEKKQREEEK
TAYERLCKAM KDVLGDKVEK VVVSERLATS PCILVTSEFG WSAHMEQIMR NQALRDSSMS
AYMMSKKTME INPAHPIVKE LKRRVEADEN DKAVKDLVYL LFDTALLTSG FTLDDPTSYA
ERIHRMIKLG LSLDDEDNGN EEAEPAAAVP AEPVAGTSSM EQVD
