Q8L7Z3 · DRE2_ARATH
- ProteinAnamorsin homolog
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids272 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 195 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 202 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 205 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 207 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 233 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 236 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 244 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 247 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial intermembrane space | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | electron transfer activity | |
Molecular Function | metal ion binding | |
Biological Process | iron-sulfur cluster assembly |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAnamorsin homolog
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8L7Z3
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000392333 | 1-272 | Anamorsin homolog | |||
Sequence: MDSMMNQKTVLAVTDDVVLPVSSVLAIMKELGKEVIESFDPLIITQASTINQFPLDASSVEAVLAISKTSDFPSDKICGEFSRILKPGGTVSVCKVLEGETGEIQQTIQRRVTLAGFLEPQCLDLKSIKLSTFSLSFGIKAKKPSWKIGSSFALKKPVTNLFKIDLDDDVDLIDEDSLLTEEDLMKPQLPVASGCETTKKACKNCVCGRAEIEEKAVKLGLTEDQIENPQSSCGSCGLGDAFRCGTCPYKGLPPFKLGEKVTLSQNFLEADI |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-156 | N-terminal SAM-like domain | ||||
Sequence: MDSMMNQKTVLAVTDDVVLPVSSVLAIMKELGKEVIESFDPLIITQASTINQFPLDASSVEAVLAISKTSDFPSDKICGEFSRILKPGGTVSVCKVLEGETGEIQQTIQRRVTLAGFLEPQCLDLKSIKLSTFSLSFGIKAKKPSWKIGSSFALKK | ||||||
Region | 157-185 | Linker | ||||
Sequence: PVTNLFKIDLDDDVDLIDEDSLLTEEDLM | ||||||
Region | 195-207 | Fe-S binding site A | ||||
Sequence: CETTKKACKNCVC | ||||||
Motif | 233-236 | Cx2C motif 1 | ||||
Sequence: CGSC | ||||||
Region | 233-247 | Fe-S binding site B | ||||
Sequence: CGSCGLGDAFRCGTC | ||||||
Motif | 244-247 | Cx2C motif 2 | ||||
Sequence: CGTC |
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
- Sequence statusComplete
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.
- Name1
- Length272
- Mass (Da)29,436
- Last updated2002-10-01 v1
- Checksum1A2CEA44C2BEFDD2
Q8L7Z3-2
- Name2
- Differences from canonical
- 1-3: Missing
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_042905 | 1-3 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 77 | in Ref. 3; AAL87328 | ||||
Sequence: I → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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. |