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Database: UniProt
Entry: B9RJS6_RICCO
LinkDB: B9RJS6_RICCO
Original site: B9RJS6_RICCO 
ID   B9RJS6_RICCO            Unreviewed;       494 AA.
AC   B9RJS6;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Chaperone protein DNAj, putative {ECO:0000313|EMBL:EEF48578.1};
GN   ORFNames=RCOM_1038380 {ECO:0000313|EMBL:EEF48578.1};
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).
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DR   EMBL; EQ973783; EEF48578.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9RJS6; -.
DR   STRING; 3988.B9RJS6; -.
DR   eggNOG; KOG0715; Eukaryota.
DR   InParanoid; B9RJS6; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; 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   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR   Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR   HAMAP; MF_01152; DnaJ; 1.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR43096:SF36; CHAPERONE PROTEIN DNAJ 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00546}.
FT   DOMAIN          87..152
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          233..307
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         233..307
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
SQ   SEQUENCE   494 AA;  54988 MW;  D71CE038B937AA67 CRC64;
     MGRYGWLATL CRRRHLLSSA AVESTVNRGH WHRKISTLRQ HLCRDRCFHS CSFVIAKRSG
     CLGTAEMQSL KCRYIHATGT CNAKEPSYYE ILGVSENASQ DEIKKAFHLL AKKYHPDANK
     NNPSAKRNFQ EIREAYETLK DSEKRAQYDT RHARSSEKVE YGANFADWFG HGAEDAARFR
     YGAGNGKGFS YSYQTNFSDS FHKIFSEIFE DANQSASDIQ VELVLSFTEA ARGCTKHLSF
     DAFVPCDSCD GRGFPIDAKT RVCPACRGIG KITIPPFTST CSSCKGSGRI IEEYCMSCRG
     SGVVEGVKEV KVTVPAGIDS GDTIRVPEAG NAGGRGHQPG NLFISLKVED DPVFTRDGVD
     VYVDANISFT QAILGGKVDV PTLSGKFQIK IPKGVQPGQL LVLRGKGLPK HGFLVDHGDQ
     FVRFRINFPT AINERQRAIL EEFALEEINN ENGTSNEGNW WQHLLERVTE PNKLRRNQTL
     LTDTCFSRGA EKND
//
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