ID   U5QB52_9APIC            Unreviewed;       800 AA.
AC   U5QB52;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Heat shock protein 90 HtpG {ECO:0000313|EMBL:AGY56137.1};
OS   Babesia orientalis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=273649 {ECO:0000313|EMBL:AGY56137.1};
RN   [1] {ECO:0000313|EMBL:AGY56137.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24970594; DOI=10.1186/1756-3305-7-293;
RA   Khan M.K., He L., Zhang W., Wang Y., Tao Q., Song Q., Sajid M.S., Yu Q.,
RA   Hu J., Fang R., Hu M., Zhou Y., Zhao J.;
RT   "Identification of two novel HSP90 proteins in Babesia orientalis:
RT   molecular characterization, and computational analyses of their structure,
RT   function, antigenicity and inhibitor interaction.";
RL   Parasit. Vectors 7:293-293(2014).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; KF379584; AGY56137.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5QB52; -.
DR   SMR; U5QB52; -.
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; 3.40.50.11260; -; 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   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_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11528:SF41; HEAT SHOCK PROTEIN 90-6, MITOCHONDRIAL; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
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.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Stress response {ECO:0000313|EMBL:AGY56137.1}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..800
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004663817"
FT   DOMAIN          142..307
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
SQ   SEQUENCE   800 AA;  91028 MW;  7D2C76F1F656AE39 CRC64;
     MTAGGALRGV QAARWTFYVL LAALCIYSAN AFNIKPKDIG SLHPRLKKQQ MDLGSGHTSR
     PLYGFFSSDS GENTDGIKGS MQQKIGLTAE AESLDTAKIT RYDKELNLDS PEPQVKVQNE
     QTFPFQAEVS RVMDIIVNSL YTDKDIFLRE LVSNAADALD KRRIKADPDE KVPREAFGGI
     RIIPDKEHNT LTIEDDGIGM TKDELVNNLG TIAESGTAKF LKQLEAGPDP DSNNLIGQFG
     VGFYSAFLVS NKVEVYSRAY GHEDGDIYRW KSETNGTFCV AQVNDPEVQK DFMKTGTRIV
     LHIKPECDDY LEDYKIKELL RKYSEFVRFP IQVWVEKVEY ERVPDESTAV EGKPGRYKTI
     SKKRHEWEHV NTQIPIWRRD QADVKPEDYV SFYKSTFKAY DDPLSYIHFK VEGQVEFSCL
     LFVPGSLPWE LSRNMFDDQS RGIRLYVKRV FINDKFSEAV PRWLTFVRGV VDSDELALNV
     GREYLQRSKA LTIINKRIAT KAIDMFKNLQ SATPERFKKF SDHFGKYIKI GVVEDRENQQ
     DLASLVTFWS TNSGQDRITL DEYVKRMKPK QPAIYYLTAD NMQAAQSSPS LEKLKALDYE
     VLYALEPVDE FCFSSLTASK YKNIMVLDVN KSDLKLNEPE AKEGQPPKEN EVEYETLCSW
     LKQLFPDDVH DVKISKRLVE SPAILVQTDF GLSPSMQRYM KQQATSAGMN DTELFGTSMV
     SKPVLEINVD HPIIQHLNLM VKADKLSDVP RQVAKQLLDV VSIQGGYNVK NPTLFAKNVL
     QLMQREAKQF LEKQSPTVAA
//