Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana (thale cress)] - Gene

Summary

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Official Full Name: Chaperone DnaJ-domain superfamily protein
Primary source: TAIR:AT4G07990
Locus tag: AT4G07990
See related: Araport:AT4G07990
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Arabidopsis thaliana (ecotype: Columbia)
Lineage: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
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Genomic context

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See in Genome Data Viewer

Location:: chromosome: 4

Exon count:: 7

Sequence:: Chromosome: 4; NC_003075.7 (4824624..4829167, complement)

Chromosome 4 - NC_003075.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003075.7

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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NM_001340570.1

Supported by ESTs:

NM_116868.4

Supported by ESTs:

Gene Ontology Provided by TAIR

Function	Evidence Code	Pubs
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
acts_upstream_of_or_within defense response	IEP Inferred from Expression Pattern more info	PubMed

Component	Evidence Code	Pubs
located_in chloroplast	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	ISM Inferred from Sequence Model more info

General protein information

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Preferred Names: Chaperone DnaJ-domain superfamily protein

NP_001319878.1

Chaperone DnaJ-domain superfamily protein; FUNCTIONS IN: heat shock protein binding; INVOLVED IN: protein folding; EXPRESSED IN: 22 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: Molecular chaperone, heat shock protein, Hsp40, DnaJ (InterPro:IPR015609), Heat shock protein DnaJ, N-terminal (InterPro:IPR001623); BEST Arabidopsis thaliana protein match is: Chaperone DnaJ-domain superfamily protein (TAIR:AT5G18140.1).

NP_567329.2

Chaperone DnaJ-domain superfamily protein; FUNCTIONS IN: heat shock protein binding; INVOLVED IN: protein folding; EXPRESSED IN: 22 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: Molecular chaperone, heat shock protein, Hsp40, DnaJ (InterPro:IPR015609), Heat shock protein DnaJ, N-terminal (InterPro:IPR001623); BEST Arabidopsis thaliana protein match is: Chaperone DnaJ-domain superfamily protein (TAIR:AT5G18140.1); Has 30201 Blast hits to 17322 proteins in 780 species: Archae - 12; Bacteria - 1396; Metazoa - 17338; Fungi - 3422; Plants - 5037; Viruses - 0; Other Eukaryotes - 2996 (source: NCBI BLink).

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003075.7 Reference assembly

Range

4824624..4829167 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001340569.1 → NP_001319878.1 Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Status: REVIEWED

UniProtKB/TrEMBL

A0A178UWL6, Q8L814, Q8LGD2

Conserved Domains (1) summary

smart00271
Location:153 → 214

DnaJ; DnaJ molecular chaperone homology domain
NM_116868.4 → NP_567329.2 Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

See identical proteins and their annotated locations for NP_567329.2

Status: REVIEWED

UniProtKB/TrEMBL

A0A178UUJ6, F4JG06, Q8LGD2

Conserved Domains (1) summary

smart00271
Location:167 → 228

DnaJ; DnaJ molecular chaperone homology domain
NM_001340570.1 → NP_001329901.1 Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Status: REVIEWED

UniProtKB/TrEMBL

A0A1P8B941, Q8LGD2

Conserved Domains (2) summary

PRK09430
Location:113 → 186

djlA; co-chaperone DjlA

cl02542
Location:153 → 193

DnaJ; DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, ...