A0A9W5WWN0 · A0A9W5WWN0_BABOV
- ProteinAnamorsin homolog
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids250 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 a FAD- and FMN-containing diflavin oxidoreductase. 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.
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 183 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 190 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 193 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 195 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 219 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 222 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 230 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 233 | [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
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia
Accessions
- Primary accessionA0A9W5WWN0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 66-135 | Fe-S cluster assembly protein Dre2 N-terminal | ||||
Sequence: SSNLKESTYDHVLLVADSTFCSTGADVSQLLEKLHDALKANGTLCIHLPPTNKNEKLLKKECMYSGFVDV | ||||||
Domain | 206-248 | Anamorsin C-terminal | ||||
Sequence: NTVESNVDAPTSSCGNCYLGDAFRCANCPYKGLPAFSPGDKVV | ||||||
Motif | 219-222 | Cx2C motif 1 | ||||
Sequence: CGNC | ||||||
Region | 219-233 | Fe-S binding site B | ||||
Sequence: CGNCYLGDAFRCANC | ||||||
Motif | 230-233 | Cx2C motif 2 | ||||
Sequence: CANC |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length250
- Mass (Da)27,090
- Last updated2023-11-08 v1
- Checksum235F720C50ECD340
Keywords
- Technical term