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Database: UniProt
Entry: Q4U901_THEAN
LinkDB: Q4U901_THEAN
Original site: Q4U901_THEAN 
ID   Q4U901_THEAN            Unreviewed;       655 AA.
AC   Q4U901;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Heat-shock (HSP70 homologue) protein, putative {ECO:0000313|EMBL:CAI76702.1};
GN   ORFNames=TA10500 {ECO:0000313|EMBL:CAI76702.1};
OS   Theileria annulata.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI76702.1, ECO:0000313|Proteomes:UP000001950};
RN   [1] {ECO:0000313|EMBL:CAI76702.1, ECO:0000313|Proteomes:UP000001950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
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   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; CR940353; CAI76702.1; -; Genomic_DNA.
DR   RefSeq; XP_953327.1; XM_948234.1.
DR   AlphaFoldDB; Q4U901; -.
DR   STRING; 5874.Q4U901; -.
DR   GeneID; 3862684; -.
DR   KEGG; tan:TA10500; -.
DR   VEuPathDB; PiroplasmaDB:TA10500; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   InParanoid; Q4U901; -.
DR   OMA; DSKPCIE; -.
DR   OrthoDB; 3028330at2759; -.
DR   Proteomes; UP000001950; Chromosome 4.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001950};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..655
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004244846"
FT   REGION          636..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          283..310
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          538..565
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   655 AA;  72819 MW;  156A0CA328268A0B CRC64;
     MNIVNKLRRK YVSFIIYVLI LKLTTCKPET TGRIEGPVIG IDLGTTFSCV GVYKNGRVEI
     IADENGDRIT PSYVSFVDGH HKIGMAAKNE ATVHAEKTVF DVKRLIGREF HDPDVQNDMK
     NLPYTIINKK NRPYVRVNDT ETKEYAPEEI SAMVLSRMKS LAEAYLGKEV KKAIITVPAY
     FNDSQRQSTK DAGTIAGLDV IRIINEPTAA AIAYGIDKTN EESNILVYDL GGGTFDVSLL
     SLDSGVFEVI ATGGDTHLGG EDFDRRVMDH FINIFKQKTG LNVRDDKRAL QKLRKEVEAA
     KRQLSTKTEV TVEIEDLLDG KDFSETLTRA KFEALNEDLF DKTMDTVKSV LKEAKMTKSD
     INQIVLVGGS TRIPKVREMI RDYFNKEPDV SINADEAVAY GAAMQGGILT GESSQDLLLL
     DVCPLSLGIE TVGGVMSKII ERNTMIPANK SQIFSTYSDN QTVVTINVFQ GERPLTKDNV
     PLGKFDLTGI PPAPKGVPQI EVTFNIDTNG ILSVTAQEKG SGNTKNLVIE PKSGRLSQEE
     IERMVRDAEE NAEKDKEVAD KIMSKQSLEN YIDSMRRTLK EESVSSKLSK SEVTKLKEEL
     DDASNWLGSH PDEEAQEYKD KLSHLESVCS PVVSKLYSQQ HKDTEQEDAS YSEEL
//
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