GenomeNet

Database: UniProt
Entry: Q0JB88
LinkDB: Q0JB88
Original site: Q0JB88 
ID   DJA6_ORYSJ              Reviewed;         416 AA.
AC   Q0JB88; B0FFN7; Q7X6U9;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Chaperone protein dnaJ A6 {ECO:0000305};
DE            Short=OsDjA6 {ECO:0000303|PubMed:23160806};
GN   Name=DJA6 {ECO:0000303|PubMed:23160806};
GN   Synonyms=RNB8 {ECO:0000303|PubMed:19130198};
GN   OrderedLocusNames=Os04g0549600 {ECO:0000312|EMBL:BAF15399.1},
GN   LOC_Os04g46390 {ECO:0000305};
GN   ORFNames=OsJ_15688 {ECO:0000312|EMBL:EEE61449.1},
GN   OSJNBb0034G17.1 {ECO:0000312|EMBL:CAD41609.2};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wuyujing 3;
RA   Lu L.M., Qin M.L., Lan H.H., Wang P., Niu X.Q., Wu Z.J., Xie L.H.;
RT   "Construction and characterization of a yeast two-hybrid cDNA library from
RT   rice seedling leaves.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH RICE STRIPE VIRUS PC4 AC_Q00847.
RX   PubMed=19130198; DOI=10.1007/s11262-008-0324-z;
RA   Lu L., Du Z., Qin M., Wang P., Lan H., Niu X., Jia D., Xie L., Lin Q.,
RA   Xie L., Wu Z.;
RT   "Pc4, a putative movement protein of Rice stripe virus, interacts with a
RT   type I DnaJ protein and a small Hsp of rice.";
RL   Virus Genes 38:320-327(2009).
RN   [9]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=23160806; DOI=10.1007/s12192-012-0384-9;
RA   Sarkar N.K., Thapar U., Kundnani P., Panwar P., Grover A.;
RT   "Functional relevance of J-protein family of rice (Oryza sativa).";
RL   Cell Stress Chaperones 18:321-331(2013).
RN   [10]
RP   FUNCTION, INTERACTION WITH ZFP1, SUBCELLULAR LOCATION, AND INDUCTION BY THE
RP   RICE BLAST FUNGUS.
RX   PubMed=28220688; DOI=10.1111/mpp.12546;
RA   Zhong X., Yang J., Shi Y., Wang X., Wang G.L.;
RT   "The DnaJ protein OsDjA6 negatively regulates rice innate immunity to the
RT   blast fungus Magnaporthe oryzae.";
RL   Mol. Plant Pathol. 19:607-614(2018).
CC   -!- FUNCTION: Involved in disease resistance. Acts as a negative regulator
CC       of innate immunity to the rice blast fungus (Magnaporthe oryzae). Acts
CC       as a negative regulator of the pathogen-associated molecular pattern
CC       (PAMP)-triggered immunity (PTI) response through the inhibition of
CC       reactive oxygen species (ROS) accumulation and expression of defense-
CC       related genes. May function via the ubiquitin-proteasome degradation
CC       pathway. {ECO:0000269|PubMed:28220688}.
CC   -!- SUBUNIT: Interacts with ZFP1. {ECO:0000269|PubMed:28220688}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28220688}. Cytoplasm
CC       {ECO:0000269|PubMed:28220688}.
CC   -!- INDUCTION: Induced by a compatible race of the rice blast fungus
CC       (Magnaporthe oryzae). {ECO:0000269|PubMed:28220688}.
CC   -!- MISCELLANEOUS: Plants silencing DJA6 display enhanced resistance to the
CC       rice blast fungus (Magnaporthe oryzae) and accumulate increased levels
CC       of reactive oxygen species after elicitation with flagellin (flg22) or
CC       chitin oligomer. {ECO:0000269|PubMed:28220688}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD41609.2; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: Os04g0549500 and Os04g0549600.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU325987; ABY52936.1; -; mRNA.
DR   EMBL; AL663000; CAD41609.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008210; BAF15399.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS90366.1; -; Genomic_DNA.
DR   EMBL; CM000141; EEE61449.1; -; Genomic_DNA.
DR   EMBL; AK101956; BAG95310.1; -; mRNA.
DR   RefSeq; XP_015635751.1; XM_015780265.1.
DR   RefSeq; XP_015635752.1; XM_015780266.1.
DR   AlphaFoldDB; Q0JB88; -.
DR   SMR; Q0JB88; -.
DR   STRING; 39947.Q0JB88; -.
DR   PaxDb; 39947-Q0JB88; -.
DR   EnsemblPlants; Os04t0549600-01; Os04t0549600-01; Os04g0549600.
DR   GeneID; 4336584; -.
DR   Gramene; Os04t0549600-01; Os04t0549600-01; Os04g0549600.
DR   KEGG; osa:4336584; -.
DR   eggNOG; KOG0712; Eukaryota.
DR   HOGENOM; CLU_017633_10_2_1; -.
DR   InParanoid; Q0JB88; -.
DR   OMA; DRCKQCD; -.
DR   OrthoDB; 2785358at2759; -.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000007752; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   ExpressionAtlas; Q0JB88; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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   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; IPR044713; DNJA1/2-like.
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; PTHR43888:SF36; CHAPERONE PROTEIN DNAJ A6; 1.
DR   PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-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   1: Evidence at protein level;
KW   Cytoplasm; Host-virus interaction; Metal-binding; Nucleus; Plant defense;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..416
FT                   /note="Chaperone protein dnaJ A6"
FT                   /id="PRO_0000440256"
FT   DOMAIN          12..73
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REPEAT          146..153
FT                   /note="CXXCXGXG motif 1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          162..169
FT                   /note="CXXCXGXG motif 2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          189..196
FT                   /note="CXXCXGXG motif 3"
FT                   /evidence="ECO:0000305"
FT   ZN_FING         133..217
FT                   /note="CR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT   REGION          380..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT   CONFLICT        403
FT                   /note="D -> N (in Ref. 1; ABY52936)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   416 AA;  47148 MW;  25C8A4BB1EABA12A CRC64;
     MFGRVPRSNN TKYYEVLGVP KTASKDELKK AYRKAAIKNH PDKGGDPEKF KELSQAYEVL
     TDPEKRDIYD QYGEDALKDG MGGGSDFHNP FDIFEQFFGG GAFGGSSSRV RRQRRGEDVA
     HTLKVSLEDV YNGSMKKLSL SRNILCPKCK GKGTKSEAPA TCYGCHGVGM RNIMRQIGLG
     MIQHMQTVCP ECRGSGEIIS DRDKCTNCRA SKVIQEKKVL EVHIEKGMQH GQKIVFQGEA
     DEAPDTVTGD IVFILQVKVH PRFKRKYDDL FIERTISLTE ALCGFQFILT HLDSRQLLIK
     ANPGEIIKPG QHKAINDEGM PHHGRPFMKG RLFVEFNVEF PESGVLSRDQ CRALEMILPP
     KPGHQLSDMD LDQCEETTMH DVNIEEEMRR KQYQRKQEAY DEDEEEDAPR VQCAQQ
//
DBGET integrated database retrieval system