ID   B9SP17_RICCO            Unreviewed;       647 AA.
AC   B9SP17;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Heat shock protein, putative {ECO:0000313|EMBL:EEF34649.1};
DE            EC=1.3.1.74 {ECO:0000313|EMBL:EEF34649.1};
GN   ORFNames=RCOM_1248100 {ECO:0000313|EMBL:EEF34649.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; EQ974058; EEF34649.1; -; Genomic_DNA.
DR   RefSeq; XP_002527736.1; XM_002527690.2.
DR   AlphaFoldDB; B9SP17; -.
DR   STRING; 3988.B9SP17; -.
DR   GeneID; 8279580; -.
DR   KEGG; rcu:8279580; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   InParanoid; B9SP17; -.
DR   OrthoDB; 3028330at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
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; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 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; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375:SF479; HEAT SHOCK PROTEIN 70; 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; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Oxidoreductase {ECO:0000313|EMBL:EEF34649.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Stress response {ECO:0000313|EMBL:EEF34649.1}.
FT   REGION          622..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   647 AA;  70921 MW;  1D4E941E4FDCAEBD CRC64;
     MAGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDT ERLIGDAAKN
     QVAMNPVNTV FDAKRLIGRR FTDASVQSDI KLWPFKVIPG PGDKPMIIVS YKGEDKQFAA
     EEISSMVLIK MREIAEAYLG STVKNAVVTV PAYFNDSQRQ ATKDAGVIAG LNVMRIINEP
     TAAAIAYGLD KKATSVGEKN VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD
     NRMVNHFVQE FKRKNKKDIS GNPRALRRLR TSCERAKRTL SSTAQTTIEI DSLYEGIDFY
     STITRARFEE LNMDLFRKCM EPVEKCLRDA KMDKSTVHDV VLVGGSTRIP KVQQLLQDFF
     NGKELCKSIN PDEAVAYGAA VQAAILSGEG NEKVQDLLLL DVTPLSLGLE TAGGVMTVLI
     PRNTTIPTKK EQVFSTYSDN QPGVLIQVYE GERTRTRDNN LLGKFELSGI PPAPRGVPQI
     TVCFDIDANG ILNVSAEDKT TGQKNKITIT NDKGRLSKEE IEKMVQEAEK YKSEDEEHKK
     KVEAKNALEN YAYNMRNTVK DEKIGAKLSP ADKKKIEDAI ESAIQWLDSN QLAEADEFED
     KMKELESICN PIIAKMYQGA GGEMGAGMDE DAPAGGSGAG PKIEEVD
//