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Database: UniProt
Entry: M5XMX7_PRUPE
LinkDB: M5XMX7_PRUPE
Original site: M5XMX7_PRUPE 
ID   M5XMX7_PRUPE            Unreviewed;       569 AA.
AC   M5XMX7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Heat shock 70 kDa protein 8 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PRUPE_1G012200 {ECO:0000313|EMBL:ONI26242.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI26242.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI26242.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
RN   [2] {ECO:0000313|EMBL:ONI26242.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Verde I., Jenkins J., Dondini L., Micali S., Pagliarani G., Vendramin E.,
RA   Paris R., Aramini V., Gazza L., Rossini L., Bassi D., Troggio M., Shu S.,
RA   Grimwood J.H., Tartarini S., Dettori M.T., Schmutz J.;
RT   "WGS assembly of Prunus persica.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; CM007651; ONI26242.1; -; Genomic_DNA.
DR   EMBL; CM007651; ONI26243.1; -; Genomic_DNA.
DR   RefSeq; XP_007225647.1; XM_007225585.1.
DR   AlphaFoldDB; M5XMX7; -.
DR   STRING; 3760.M5XMX7; -.
DR   EnsemblPlants; ONI26242; ONI26242; PRUPE_1G012200.
DR   EnsemblPlants; ONI26243; ONI26243; PRUPE_1G012200.
DR   GeneID; 18791528; -.
DR   Gramene; ONI26242; ONI26242; PRUPE_1G012200.
DR   Gramene; ONI26243; ONI26243; PRUPE_1G012200.
DR   KEGG; pper:18791528; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   HOGENOM; CLU_005965_0_1_1; -.
DR   OMA; ELYSGMN; -.
DR   OrthoDB; 447321at2759; -.
DR   Proteomes; UP000006882; Chromosome g1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   CDD; cd10170; HSP70_NBD; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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:SF101; HEAT SHOCK 70 KDA PROTEIN 8; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882}.
SQ   SEQUENCE   569 AA;  60856 MW;  176AC07747537911 CRC64;
     MAEPAYTVAS DSETTGEEKL SATFSETAIG IDIGTSQCSV AVWNGSQVEL LKNTRNQKMM
     RSYVTFKDEN PSGGVSSQLA NEQDVLSGAA IFNMKRLIGR VDTDPVVHSS KSLPFLVQTL
     GIGVRPLIAA LVNNVWRSTT PEEVVAIFLV ELKAMAEIRL KRPIKNVVLT IPASFSRFQL
     TRIERACAMA GLHVLRLMPE PTAVALLYAQ QNASQNTNTG SEKIALIFNM GAGYCDVAVT
     ATAGGVSQIK ALAGSAIGGE DLLQNMMRHL LPDSESLLTS CGLDDIKSVG LLRVATQEAI
     HSLSSQTNVQ VDVDLGNGTK ICKVVDRGEF EEVNQDVFDK CASLIIQCLH DAKVDTEDVS
     DVIVVGGCSY IPKIKSLVMS TCKKQELYKG MNPLEAAVSG AALEGAVASG LSDPFGSLDL
     LTIQATPLAI GIRADGNNFV PIIPRSTTMP AQKDLIFTTA HDNQAEALII VYEGEGKKVE
     ENHLLGYFKI TGIPLAPKGV PEIRVILDID ASSVLRVLAG VLMPGSHQPV NPVMGVRMPT
     VDDGHGWCAE ALNRVYGSTL DLVTVQRKI
//
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