DNJ11_ARATH
ID DNJ11_ARATH Reviewed; 161 AA.
AC Q9FYB5; O65641;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Chaperone protein dnaJ 11, chloroplastic;
DE Short=AtDjC11;
DE Short=AtJ11;
DE Flags: Precursor;
GN Name=ATJ11; Synonyms=C11, J11; OrderedLocusNames=At4g36040;
GN ORFNames=T19K4.170;
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 [MRNA], PROTEIN SEQUENCE OF 37-55, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11516154; DOI=10.1023/a:1010665702621;
RA Orme W., Walker A.R., Gupta R., Gray J.C.;
RT "A novel plastid-targeted J-domain protein in Arabidopsis thaliana.";
RL Plant Mol. Biol. 46:615-626(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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).
CC -!- FUNCTION: Plays a continuous role in plant development probably in the
CC structural organization of compartments. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:11516154}. Note=Probably also in other plastids.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC developing siliques. {ECO:0000269|PubMed:11516154}.
CC -!- SIMILARITY: Belongs to the DnaJ family. C/III subfamily. {ECO:0000305}.
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DR EMBL; AJ292973; CAC03599.1; -; mRNA.
DR EMBL; AL022373; CAA18498.1; -; Genomic_DNA.
DR EMBL; AL161588; CAB81513.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86605.1; -; Genomic_DNA.
DR PIR; T05496; T05496.
DR RefSeq; NP_195328.1; NM_119771.4.
DR AlphaFoldDB; Q9FYB5; -.
DR SMR; Q9FYB5; -.
DR STRING; 3702.AT4G36040.1; -.
DR PaxDb; Q9FYB5; -.
DR PRIDE; Q9FYB5; -.
DR ProteomicsDB; 222078; -.
DR EnsemblPlants; AT4G36040.1; AT4G36040.1; AT4G36040.
DR GeneID; 829760; -.
DR Gramene; AT4G36040.1; AT4G36040.1; AT4G36040.
DR KEGG; ath:AT4G36040; -.
DR Araport; AT4G36040; -.
DR TAIR; locus:2135159; AT4G36040.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_9_1_1; -.
DR InParanoid; Q9FYB5; -.
DR OMA; MINTSAP; -.
DR OrthoDB; 1419673at2759; -.
DR PhylomeDB; Q9FYB5; -.
DR PRO; PR:Q9FYB5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FYB5; baseline and differential.
DR Genevisible; Q9FYB5; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:11516154"
FT CHAIN 37..161
FT /note="Chaperone protein dnaJ 11, chloroplastic"
FT /id="PRO_0000007266"
FT DOMAIN 65..133
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 149
FT /note="S -> R (in Ref. 1; CAC03599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 17822 MW; 8299FA09B85B2E51 CRC64;
MLSSSPTSFT HPFLSSSPPL SPISPPSRTA RISPPLVSAS CSYTYTEDSP RLHQIPRRLT
TVPASLYDVL EVPLGATSQD IKSAYRRLAR ICHPDVAGTD RTSSSSADEF MKIHAAYCTL
SDPEKRSVYD RRMLRRSRPL TVGTSGLGSY VGRNWETDQC W
