ID U6JST6_9EIME Unreviewed; 490 AA.
AC U6JST6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Heat shock protein 90, putative {ECO:0000313|EMBL:CDJ27836.1};
GN ORFNames=EMH_0035290 {ECO:0000313|EMBL:CDJ27836.1};
OS Eimeria mitis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=44415 {ECO:0000313|EMBL:CDJ27836.1};
RN [1] {ECO:0000313|EMBL:CDJ27836.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ27836.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ27836.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ27836.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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; HG680320; CDJ27836.1; -; Genomic_DNA.
DR RefSeq; XP_013350413.1; XM_013494959.1.
DR AlphaFoldDB; U6JST6; -.
DR EnsemblProtists; CDJ27836; CDJ27836; EMH_0035290.
DR GeneID; 25378321; -.
DR VEuPathDB; ToxoDB:EMH_0035290; -.
DR OrthoDB; 214075at2759; -.
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 Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
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 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 PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR PROSITE; PS00298; HSP90; 2.
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 Stress response {ECO:0000313|EMBL:CDJ27836.1}.
FT REGION 62..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 52260 MW; 7B8F4778A2391A4B CRC64;
MVSKPLLQHS PLLLVQQQQQ QQQQQLLLLL LLPQLARPSV TKSFRVLLQQ QQQQQQQQQQ
QQQQQQQQQQ QQQHGDDAAA PPPAAAAAAD TAAAAAASDE GPKGPVDTLE SIPELQGRED
EKIETHEYQA EVTRLMDIII NSLYTQRDVF LRELISNAVD ALEKARFLSL TSETNTSSSS
SSSSSSSSSK GAELAVYIEA DPQKKMLSIC DTGVGMSKQE LITNLGTVAN GDDAAAPAAA
AAADSAAAAA AAAAAAAGDD EGPKGPVDTL ESIPELQGRE DEKIETHEYQ AEVTRLMDII
INSLYTQRDV FLRELISNAV DALEKARFLS LTSETNSSSS SSSSSSKAAE LAVYIEADPQ
KKMLSICDTG VGMSKQELIT NLGTVAKSGT NNFLESVLAN SSSSKDSSSS SSSSSSSGGG
DVSLVGQFGV GFYSAFLVAD RVRVISRAAG EEQYIWESTA DAKYYINKDP RGKTMNRGEE
EDEDGGKRGV
//
