ID   A0A0E0GE88_ORYNI        Unreviewed;       487 AA.
AC   A0A0E0GE88;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=J domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA02G38430.1};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA02G38430.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA02G38430.1};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA02G38430.1}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA02G38430.1};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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DR   AlphaFoldDB; A0A0E0GE88; -.
DR   STRING; 4536.A0A0E0GE88; -.
DR   EnsemblPlants; ONIVA02G38430.1; ONIVA02G38430.1; ONIVA02G38430.
DR   Gramene; ONIVA02G38430.1; ONIVA02G38430.1; ONIVA02G38430.
DR   eggNOG; KOG0715; Eukaryota.
DR   HOGENOM; CLU_017633_0_1_1; -.
DR   OMA; EKVRIRH; -.
DR   Proteomes; UP000006591; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
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; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   CDD; cd10719; DnaJ_zf; 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   NCBIfam; TIGR02349; DnaJ_bact; 1.
DR   PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43096:SF22; MOLECULAR CHAPERONE HSP40_DNAJ FAMILY PROTEIN; 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:UP000006591};
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          71..135
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          205..287
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         205..287
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  52083 MW;  E70FC2B4F2B113EB CRC64;
     MALATSTLPF APSNPSPSSR SAAAAFSPRG GVHFAAARSG LPLACAAPRH RGRPPPRRRR
     GGCLVVWASA DYYATLGVPR SASNKDIKAA YRKLARQYHP DVNKEPGATD KFKEISAAYE
     VLSDEKKRAL YDQYGEAGVR SAVGGSAGAY TSNPFDLFET FFGASMGGFS GMDQGTFRTR
     RRSTAVQGED IRYDVNLGFS EAIFGTEKDI ILSHLETCDA CAGSGSKIGS KMRICSTCGG
     RGQVMRTEQT PFGLFSQVSI CPTCAGEGEV ISEYCKKCAG EGRVRVRKEI KVKIPPGVSK
     GSTLRVRGEG DAGPKGGPPG DLFVCLDIEE PADIKRDGIN LYSTVSVSYI EAILGTVKKV
     RTVDGNSELR IPPGTQPGDV VVLAKQGVPS LNKPSVRGDH LFTIKVTIPK RISGREKELL
     EELASLSNGG FARAPVKPKS IRQENETTVA QENSDQPDEG EGDWLKKLQD FAGSIANGAA
     KWLKDNL
//