Q8L7Z3 · DRE2_ARATH

Function

function

Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via FAD- and FMN-containing diflavin oxidoreductase TAH18/ATR3 (PubMed:23754812).
Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity).
Required for embryo development (PubMed:23754812).

Cofactor

Protein has several cofactor binding sites:
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Features

Showing features for binding site.

127220406080100120140160180200220240260
TypeIDPosition(s)Description
Binding site195[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site202[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site205[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site207[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site233[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site236[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site244[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site247[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial intermembrane space
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionelectron transfer activity
Molecular Functionmetal ion binding
Biological Processiron-sulfur cluster assembly

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Anamorsin homolog
  • Alternative names
    • Fe-S cluster assembly protein DRE2 homolog

Gene names

    • ORF names
      F20L16.120
    • Ordered locus names
      At5g18400

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q8L7Z3
  • Secondary accessions
    • F4JWM7
    • Q8L9M1
    • Q8RXJ2

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003923331-272Anamorsin homolog

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Monomer (By similarity).
Interacts with ATR3 (PubMed:20406405).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, motif.

TypeIDPosition(s)Description
Region1-156N-terminal SAM-like domain
Region157-185Linker
Region195-207Fe-S binding site A
Motif233-236Cx2C motif 1
Region233-247Fe-S binding site B
Motif244-247Cx2C motif 2

Domain

The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters.
The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.

Sequence similarities

Belongs to the anamorsin family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8L7Z3-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    272
  • Mass (Da)
    29,436
  • Last updated
    2002-10-01 v1
  • Checksum
    1A2CEA44C2BEFDD2
MDSMMNQKTVLAVTDDVVLPVSSVLAIMKELGKEVIESFDPLIITQASTINQFPLDASSVEAVLAISKTSDFPSDKICGEFSRILKPGGTVSVCKVLEGETGEIQQTIQRRVTLAGFLEPQCLDLKSIKLSTFSLSFGIKAKKPSWKIGSSFALKKPVTNLFKIDLDDDVDLIDEDSLLTEEDLMKPQLPVASGCETTKKACKNCVCGRAEIEEKAVKLGLTEDQIENPQSSCGSCGLGDAFRCGTCPYKGLPPFKLGEKVTLSQNFLEADI

Q8L7Z3-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-3: Missing

Sequence caution

The sequence AAM65895.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0429051-3in isoform 2
Sequence conflict77in Ref. 3; AAL87328

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC051626
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CP002688
EMBL· GenBank· DDBJ
AED92550.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED92551.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED92552.1
EMBL· GenBank· DDBJ
Genomic DNA
AY080855
EMBL· GenBank· DDBJ
AAL87328.1
EMBL· GenBank· DDBJ
mRNA
AY123986
EMBL· GenBank· DDBJ
AAM74499.1
EMBL· GenBank· DDBJ
mRNA
BT000943
EMBL· GenBank· DDBJ
AAN41343.1
EMBL· GenBank· DDBJ
mRNA
BT001035
EMBL· GenBank· DDBJ
AAN46789.1
EMBL· GenBank· DDBJ
mRNA
AY088356
EMBL· GenBank· DDBJ
AAM65895.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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