ID U6L4F2_EIMTE Unreviewed; 774 AA.
AC U6L4F2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Heat shock protein 90, putative {ECO:0000313|EMBL:CDJ42655.1};
GN ORFNames=ETH_00033250 {ECO:0000313|EMBL:CDJ42655.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ42655.1};
RN [1] {ECO:0000313|EMBL:CDJ42655.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ42655.1};
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:CDJ42655.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ42655.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; HG675730; CDJ42655.1; -; Genomic_DNA.
DR RefSeq; XP_013233405.1; XM_013377951.1.
DR AlphaFoldDB; U6L4F2; -.
DR EnsemblProtists; CDJ42655; CDJ42655; ETH_00033250.
DR GeneID; 25255716; -.
DR VEuPathDB; ToxoDB:ETH2_1000200; -.
DR VEuPathDB; ToxoDB:ETH_00033250; -.
DR OMA; DHTQQNE; -.
DR OrthoDB; 5485387at2759; -.
DR GO; GO:0005739; C:mitochondrion; 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; 3.40.50.11260; -; 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; 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:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Stress response {ECO:0000313|EMBL:CDJ42655.1}.
FT REGION 583..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 85846 MW; 6D2F3DF9B299F593 CRC64;
MKRVQPSILQ RQLLASLFSI CPRDAVVATK GSRLGPLRVT RGSSLSVAAT NSIVSAAATD
PNMASSRMWL PACGDLTLKE GFRRFTATAS PAEATAGGVE GEEQSYPFQA ETQKLLQIVA
HSLYTDKEVF IRELISNASD ALEKFRFLQA TQQQQQEGDQ KQQQGQLRVI LRVNPSERTF
VIEDNGVGMN RDELVKNLGT IARSGSLEFL KNAGAEASKD IIGQFGVGFY SSFVVSDRVE
VFTRSREGGK VLRWCSDGSG TFSLSSAPAD SLSSASGTKI VCHLKQDCLE FANPHRVKEC
AKKFSSFVNF PVYMEENGKE VQISSQEALW LKPSPTPEEH KQFFRHLTNQ SWGEPFYSIM
FSADAPLCIR SVLYFPADPP NRLFQTGPLE SGVSLLARRV LVKKSATDLL PKWLWFLRGI
VDCEDLPLNV SREHMQDSVL QRKLSTVIVK RILKFLNDQV KSDPEKYRQF YQKYSQSIKE
GVLEDAHHDS VYKDMLLPLL RFECSSEDAG KMITFDEYLE KMPAKQKNIY YYCCSDRTTA
LSSPYMEQYV AKGRPVLLMT ADIDEFLVMN LSEYKEKRLV AVDSPGEDAE AETADEEDEK
TAKEKEAKPK LVGEQQTELA AFVKETLTAR VTAVKFSDRL LSSPAVVSGF LSSTLRRMMK
ATLQGAPESQ LNLASLPATL ELNPSHELIT SLYHLRTSNP DVAKLLVEQL YDNACVAAGI
MEEPKTMVGR LNKLLSLTAQ YAYHHAGGAS QPASPSGEAA AKAEKAETSE TAQA
//
