ID A0A061J3H2_TRYRA Unreviewed; 604 AA.
AC A0A061J3H2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:ESL07857.1};
GN ORFNames=TRSC58_04450 {ECO:0000313|EMBL:ESL07857.1}, TRSC58_06794
GN {ECO:0000313|EMBL:ESL05552.1};
OS Trypanosoma rangeli SC58.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Herpetosoma.
OX NCBI_TaxID=429131 {ECO:0000313|EMBL:ESL07857.1, ECO:0000313|Proteomes:UP000031737};
RN [1] {ECO:0000313|EMBL:ESL07857.1, ECO:0000313|Proteomes:UP000031737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC58 {ECO:0000313|EMBL:ESL07857.1,
RC ECO:0000313|Proteomes:UP000031737};
RA Stoco P.H., Wagner G., Gerber A., Zaha A., Thompson C., Bartholomeu D.C.,
RA Luckemeyer D.D., Bahia D., Loreto E., Prestes E.B., Lima F.M.,
RA Rodrigues-Luiz G., Vallejo G.A., Filho J.F., Monteiro K.M., Tyler K.M.,
RA de Almeida L.G., Ortiz M.F., Siervo M.A., de Moraes M.H., Cunha O.L.,
RA Mendonca-Neto R., Silva R., Teixeira S.M., Murta S.M., Sincero T.C.,
RA Mendes T.A., Urmenyi T.P., Silva V.G., da Rocha W.D., Andersson B.,
RA Romanha A.J., Steindel M., de Vasconcelos A.T., Grisard E.C.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00037441}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESL07857.1}.
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DR EMBL; AUPL01006794; ESL05552.1; -; Genomic_DNA.
DR EMBL; AUPL01004450; ESL07857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061J3H2; -.
DR EnsemblProtists; ESL05552; ESL05552; TRSC58_06794.
DR EnsemblProtists; ESL07857; ESL07857; TRSC58_04450.
DR VEuPathDB; TriTrypDB:TRSC58_04450; -.
DR VEuPathDB; TriTrypDB:TRSC58_06794; -.
DR OrthoDB; 128853at2759; -.
DR Proteomes; UP000031737; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031737}.
FT REGION 107..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 69713 MW; 48922EA9063BD9BB CRC64;
MEALEAGGDM SMIGQFGVGF YSAYLVADRV TVVSKNNDDE AYTWESSAGG TFTVTPTPEC
DLKRGTRIVL HLKEDQQEYL EERRLKDLIK KHSEFIGYDI ELMVEKTTEK EVTDEDEDEE
AATKKEEETG EEPKVEEVKD DAEEGEKKKK TKKVKEVTQE FVVQNKHKPL WTRDPKDVTK
EEYAAFYKAI SNDWEEPLST KHFSVEGQLE FRAILFLPKR APFDMFEPNK KRNNIKLYVR
RVFIMDNCED LCPEWLGFMR GVVDSEDLPL NISRENLQQN KILKVIRKNI VKKALELFEE
IAENKEDYKK FYEQFAKNVK LGIHEDSANR KKLMELLRFH SSESGEDMTT LKDYVTRMKE
GQKCIYYVTG DSKKKLETSP FIEQARRRGF EVLFMTEPID EYVMQQVKDF EDKKFACLTK
EGVHFEETEE EKKQREEEKA AHERLCKAMK EVLGDKVEKV VVSERLATSP CILVTSEFGW
SAHMEQIMRN QALRDSSMSA YMMSKKTMEI NPTHPIVKEL KRRVEADEND KAVKDLVYLL
FDTALLTSGF ALDDPTSYAD RIHRMIKLGL SLDDDDDNGN EEVAAAPAAP VEATAGTSSM
EQVD
//