DNJA6_ARATH
ID DNJA6_ARATH Reviewed; 442 AA.
AC Q9SJZ7; Q7Y204; Q8LGF3;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Chaperone protein dnaJ A6, chloroplastic {ECO:0000305};
DE Short=atDjA6 {ECO:0000303|PubMed:23894646};
DE AltName: Full=Chaperone protein dnaJ A26 {ECO:0000303|PubMed:11599562};
DE Short=AtDjA26 {ECO:0000303|PubMed:11599562};
DE Flags: Precursor;
GN Name=DJA6 {ECO:0000303|PubMed:23894646};
GN Synonyms=ATJ26 {ECO:0000303|PubMed:23894646};
GN OrderedLocusNames=At2g22360 {ECO:0000312|Araport:AT2G22360};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599562; DOI=10.1379/1466-1268(2001)006<0209:tjdpoa>2.0.co;2;
RA Miernyk J.A.;
RT "The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and
RT diverse family of chaperones.";
RL Cell Stress Chaperones 6:209-218(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY HEAT STRESS.
RX PubMed=23894646; DOI=10.1371/journal.pone.0070384;
RA Chiu C.C., Chen L.J., Su P.H., Li H.M.;
RT "Evolution of chloroplast J proteins.";
RL PLoS ONE 8:E70384-E70384(2013).
CC -!- FUNCTION: May function together with HSC70 chaperone to assist protein
CC folding and prevent protein aggregation during heat stress in the
CC chloroplast. {ECO:0000305|PubMed:23894646}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:23894646}.
CC -!- INDUCTION: Induced by heat stress. {ECO:0000269|PubMed:23894646}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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DR EMBL; AC006592; AAD22362.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07297.1; -; Genomic_DNA.
DR EMBL; BT008670; AAP40480.1; -; mRNA.
DR EMBL; AK229509; BAF01364.1; -; mRNA.
DR EMBL; AY084303; AAM60893.1; -; mRNA.
DR PIR; G84611; G84611.
DR RefSeq; NP_565533.1; NM_127801.4.
DR AlphaFoldDB; Q9SJZ7; -.
DR SMR; Q9SJZ7; -.
DR STRING; 3702.AT2G22360.1; -.
DR PaxDb; Q9SJZ7; -.
DR PRIDE; Q9SJZ7; -.
DR ProteomicsDB; 222090; -.
DR EnsemblPlants; AT2G22360.1; AT2G22360.1; AT2G22360.
DR GeneID; 816768; -.
DR Gramene; AT2G22360.1; AT2G22360.1; AT2G22360.
DR KEGG; ath:AT2G22360; -.
DR Araport; AT2G22360; -.
DR TAIR; locus:2041258; AT2G22360.
DR eggNOG; KOG0715; Eukaryota.
DR HOGENOM; CLU_017633_0_1_1; -.
DR InParanoid; Q9SJZ7; -.
DR OMA; STWVARW; -.
DR OrthoDB; 894595at2759; -.
DR PhylomeDB; Q9SJZ7; -.
DR PRO; PR:Q9SJZ7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJZ7; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IDA:TAIR.
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; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
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 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; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR TIGRFAMs; TIGR02349; DnaJ_bact; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Chloroplast; Metal-binding; Plastid; Reference proteome; Repeat;
KW Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..82
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 83..442
FT /note="Chaperone protein dnaJ A6, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435729"
FT DOMAIN 86..150
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REPEAT 224..231
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT REPEAT 241..248
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT REPEAT 267..274
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT REPEAT 280..287
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT ZN_FING 211..292
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT CONFLICT 307
FT /note="S -> I (in Ref. 5; AAM60893)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="I -> V (in Ref. 5; AAM60893)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="K -> R (in Ref. 3; AAP40480 and 4; BAF01364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 47761 MW; C8A7D604C6444C0D CRC64;
MAIIQLGSTC VAQWSIRPQF AVRAYYPSRI ESTRHQNSSS QVNCLGASKS SMFSHGSLPF
LSMTGMSRNM HPPRRGSRFT VRADADYYSV LGVSKNATKA EIKSAYRKLA RNYHPDVNKD
PGAEEKFKEI SNAYEVLSDD EKKSLYDRYG EAGLKGAAGF GNGDFSNPFD LFDSLFEGFG
GGMGRGSRSR AVDGQDEYYT LILNFKEAVF GMEKEIEISR LESCGTCEGS GAKPGTKPTK
CTTCGGQGQV VSAARTPLGV FQQVMTCSSC NGTGEISTPC GTCSGDGRVR KTKRISLKVP
AGVDSGSRLR VRGEGNAGKR GGSPGDLFVV IEVIPDPILK RDDTNILYTC KISYIDAILG
TTLKVPTVDG TVDLKVPAGT QPSTTLVMAK KGVPVLNKSN MRGDQLVRVQ VEIPKRLSKE
EKKLIEELAD MSKNKTANST SR
