A0A9W5WWN0 · A0A9W5WWN0_BABOV

  • Protein
    Anamorsin homolog
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

TypeIDPosition(s)Description
Binding site183[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site190[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site193[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site195[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site219[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site222[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site230[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site233[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
      BaOVIS_032910

Organism names

  • Taxonomic identifier
  • Organism
    Babesia ovis
  • Strain
    • Selcuk
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia

Accessions

  • Primary accession
    A0A9W5WWN0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, motif, region.

TypeIDPosition(s)Description
Domain66-135Fe-S cluster assembly protein Dre2 N-terminal
Domain206-248Anamorsin C-terminal
Motif219-222Cx2C motif 1
Region219-233Fe-S binding site B
Motif230-233Cx2C 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    250
  • Mass (Da)
    27,090
  • Last updated
    2023-11-08 v1
  • Checksum
    235F720C50ECD340
MSSSILAVAPTRDGLEKHIRFSLLVAKQDSITSSMLKLDNVLSPLITGLDFSKDDYDYINSSTISSSNLKESTYDHVLLVADSTFCSTGADVSQLLEKLHDALKANGTLCIHLPPTNKNEKLLKKECMYSGFVDVTIFEHNDSKWARGRRPNWSATHQSKAKDAIPVASLDGYIPSAPAAESCSTKPRACANCTCGRAERERLEANTVESNVDAPTSSCGNCYLGDAFRCANCPYKGLPAFSPGDKVVLD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BLIY01000024
EMBL· GenBank· DDBJ
GFE55887.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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