ID   Q5KTX1_TRIVA            Unreviewed;       353 AA.
AC   Q5KTX1;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Cytosolic-type hsp90 {ECO:0000313|EMBL:BAD83618.1};
DE   Flags: Fragment;
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722 {ECO:0000313|EMBL:BAD83618.1};
RN   [1] {ECO:0000313|EMBL:BAD83618.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C-1:NIH {ECO:0000313|EMBL:BAD83618.1};
RX   PubMed=15496553; DOI=10.1093/molbev/msi023;
RA   Arisue N., Hasegawa M., Hashimoto T.;
RT   "Root of the Eukaryota tree as inferred from combined maximum likelihood
RT   analyses of multiple molecular sequence data.";
RL   Mol. Biol. Evol. 22:409-420(2005).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; AB092409; BAD83618.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5KTX1; -.
DR   VEuPathDB; TrichDB:TVAG_153560; -.
DR   VEuPathDB; TrichDB:TVAGG3_1025540; -.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
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; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00298; HSP90; 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}.
FT   REGION          213..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD83618.1"
FT   NON_TER         353
FT                   /evidence="ECO:0000313|EMBL:BAD83618.1"
SQ   SEQUENCE   353 AA;  41521 MW;  5C81A15950521E11 CRC64;
     ETFAFQAEIN QLMSLIINAF YTNKEIFLRE LISNASDACD KIRYDSLKNQ AILGNQKEFF
     IHIRPDKENR CLSIIDSGIG MTKSHLINNL GTIARSGTRQ FMQAIEEGAD LSLIGQFGVG
     FFSAFLVADR VVVTSHHSDD DQYIWESEAG KNFTIRRDLE GEDLIRGTRI DLYLKEDMTE
     FFEEKKLKEL IKKHSEFIQY PISLWVEKTK EEEVSDDEAE KKEDEEKKDD EIKEVEDEAE
     KKDEEKKKKK VTIVEHEWEL VNKNKPLWLR PTNEITEDEY AEFYKSISND WEKHLAVKHF
     RVEGDIGFTV LLFLPRRAPY DLFEPKKKLN NIKLYVRRVF VMDNCEDLIP EWL
//