HSP90_THEAN
ID HSP90_THEAN Reviewed; 722 AA.
AC Q4UDU8;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Heat shock protein 90;
DE Short=HSP90;
GN ORFNames=TA12105;
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara;
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; CR940348; CAI74741.1; -; Genomic_DNA.
DR RefSeq; XP_952473.1; XM_947380.1.
DR AlphaFoldDB; Q4UDU8; -.
DR SMR; Q4UDU8; -.
DR STRING; 5874.XP_952473.1; -.
DR PRIDE; Q4UDU8; -.
DR GeneID; 3862045; -.
DR KEGG; tan:TA12105; -.
DR VEuPathDB; PiroplasmaDB:TA12105; -.
DR eggNOG; KOG0019; Eukaryota.
DR InParanoid; Q4UDU8; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 924636at2759; -.
DR Proteomes; UP000001950; Chromosome 2.
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:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 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_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..722
FT /note="Heat shock protein 90"
FT /id="PRO_0000232677"
FT REGION 219..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 718..722
FT /note="TPR repeat-binding"
FT COMPBIAS 237..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 722 AA; 83825 MW; 06057681F0F67E6A CRC64;
MASKEETPDQ EVYAFNADIS QLLSLIINAF YSNKEIFLRE LISNASDALE KIRYEAIKDP
KQIEDQPDYY IRLYADKNNN TLTIEDSGIG MTKADLVNNL GTIAKSGTRA FMEALQAGSD
MSMIGQFGVG FYSAYLVADK VTVVSKNNAD DQYVWESSAS GHFTVKRDDS HEPLKRGTRL
ILHLKEDQTE YLEERRLKEL VKKHSEFISF PISLSVEKTQ ETEVTDDEAE PEEEKKLEEE
DKDKEEKVED VTDEKVTDVT EEEEKKEEKK KKKRKVTNVT REWEMLNKQK PIWMRLPTEV
TNEEYASFYK NLTNDWEDHL AVKHFSVEGQ LEFKALLFVP RRAPFDMFES RKKKNNIKLY
VRRVFIMDDC EELIPEWLSF VKGVVDSEDL PLNISRETLQ QNKILKVIRK NLVKKCLELF
NELTEKKEDF KKFYEQFSKN LKLGIHEDNA NRSKIAELLR FETTKSGDEL VSLKEYVDRM
KSDQKFVYYI TGESKQSVAS SPFLETLKAR DYEVLYMTDP IDEYAVQQIK EFEGKKLKCC
TKEGLELDEG EDEKKSFEAL KEEMEPLCKH IKEVLHDKVE KVVCGTRFTD SPCALVTSEF
GWSANMERIM KAQALRDSSI TSYMLSKKIM EINPRHSIMK ELKARAANDK TDKTVKDLVW
LLYDTALLTS GFNLDEPTQF GNRIYRMIKL GLSLDDEEHV EDDSSMPPLD EPVVDSKMEE
VD
