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Database: UniProt
Entry: Q2VA67_9APIC
LinkDB: Q2VA67_9APIC
Original site: Q2VA67_9APIC 
ID   Q2VA67_9APIC            Unreviewed;       372 AA.
AC   Q2VA67;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Heat shock 70 kDa protein {ECO:0000256|ARBA:ARBA00018181};
DE   Flags: Fragment;
OS   Theileria sp. China.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=70114 {ECO:0000313|EMBL:ABB86780.1};
RN   [1] {ECO:0000313|EMBL:ABB86780.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16425067; DOI=10.1007/s00436-005-0105-8;
RA   Miranda J., Bakheit M.A., Liu Z., Yin H., Mu Y., Guo S., Beyer D.,
RA   Oliva A., Ahmed J.S., Seitzer U.;
RT   "Development of a recombinant indirect ELISA for the diagnosis of Theileria
RT   sp. (China) infection in small ruminants.";
RL   Parasitol. Res. 98:561-567(2006).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   EMBL; DQ278176; ABB86780.1; -; mRNA.
DR   AlphaFoldDB; Q2VA67; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375:SF395; HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   REGION          149..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..345
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABB86780.1"
FT   NON_TER         372
FT                   /evidence="ECO:0000313|EMBL:ABB86780.1"
SQ   SEQUENCE   372 AA;  40332 MW;  63426CCE1ABBC0E4 CRC64;
     SVPAYFNDSQ RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKKSGGEKN VLIFDLGGGT
     FDVSILTIED GIFEVKATAG DTHLGGEDFD NLLVEHCVRD FMRLNNGKNL LDQQEGAQGA
     AHALRAREAR ALELHAGHDR AGLALRGHRL QHHHQPRALR GALQREVQEH ARARREGARV
     LGAGQAQHPR GGARGRQHQD PQDPDADQEL LQRQGALQVD QPRRGGGLRR GGAGGHPLGQ
     PVGEDPGAAA AGRRAALAGA GDGGRRDDGA HQEEHHHPHQ EEPDLHHQRG PPGGRAHPGL
     RGRARNDQGQ QPARQVPPER DRARAQGRPA DRGHLRHRRQ RHPQRHCHGQ VDGQVGARDH
     HQRQGPPQPR GD
//
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