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Database: UniProt
Entry: A0A061J3H2_TRYRA
LinkDB: A0A061J3H2_TRYRA
Original site: A0A061J3H2_TRYRA 
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
//
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