HSP70_ENCCU
ID HSP70_ENCCU Reviewed; 592 AA.
AC O96772;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Mitochondrial-type heat shock protein 70;
DE Short=mit-hsp70;
GN Name=HSP70; OrderedLocusNames=ECU11_0540;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9615449; DOI=10.1093/oxfordjournals.molbev.a025971;
RA Peyretaillade E., Broussolle V., Peyret P., Metenier G., Gouy M.,
RA Vivares C.P.;
RT "Microsporidia, amitochondrial protists, possess a 70-kDa heat shock
RT protein gene of mitochondrial evolutionary origin.";
RL Mol. Biol. Evol. 15:683-689(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- FUNCTION: May act as a chaperone.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AJ012470; CAA10035.1; -; Genomic_DNA.
DR EMBL; AL590450; CAD25964.1; -; Genomic_DNA.
DR PIR; T43807; T43807.
DR RefSeq; NP_586360.1; NM_001042193.1.
DR AlphaFoldDB; O96772; -.
DR SMR; O96772; -.
DR STRING; 284813.O96772; -.
DR PRIDE; O96772; -.
DR GeneID; 860013; -.
DR KEGG; ecu:ECU11_0540; -.
DR VEuPathDB; MicrosporidiaDB:ECU11_0540; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; O96772; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000000819; Chromosome XI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
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; Chaperone; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..592
FT /note="Mitochondrial-type heat shock protein 70"
FT /id="PRO_0000078401"
SQ SEQUENCE 592 AA; 65092 MW; F795E6B53F58777E CRC64;
MSNADAPSRK FSSSIIGIDL GTTNSCVSVI KDGKPVIIEN QEGERTTPSV VSILKDEVVV
GTQARNRILM HPRNTIFASK RLIGRKFGDP EVEKYVKGLP FDTMSHCNGD VWIRVDGKKY
SPAQIGAFVL SKLKSSAEAF LSHPVARSVI TVPAYFNDSQ RQATKDAGRI AGLDVVRVIN
EPTAAALAYG LDKSARGNIA VYDLGGGTFD ISILEVEDGV FHVKATNGDT FLGGEDLDNE
VVKFIVEDFK QKEGIDLSND VDALGRIKEG AEKIKKELSV SCTSKMEIPY ICNSQGGPKH
LCREITRSEF EQIAKKIVER TIAPCKRALA DAGLDSSDIK HVILVGGMTR MPYVRRVVKE
IFGIEPSTDI NPDEAVANGA ALQGGVLMGE IDDVLLLDVA PLSLGIELLG GVFSRVIRRN
TTIPFKETQV FSTSEDNQTE VDIKVYQGER SMVADNKYLG QIKLKSIPPL PRGVPRIEVT
FESDANGIYR VTAQDSITKE PQSLEIIPSS GLTEAEVERM VEESERLRHL DEMKRRKAEL
IVSSSELLRR PPTELERIPK NYLDRLGKVV KGEDFDLKEM EEVLLSAKKS MS