A0A8S9ZEE4 · A0A8S9ZEE4_9BILA

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 site383[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site395[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site398[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site400[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site422[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site425[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site433[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site436[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componentmitochondrial intermembrane space
Cellular Componentnuclear exosome (RNase complex)
Cellular Componentnucleolus
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Function3'-5'-RNA exonuclease activity
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionelectron transfer activity
Molecular Functionmetal ion binding
Molecular Functionsingle-stranded RNA binding
Biological Processexonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Processhistone mRNA catabolic process
Biological Processiron-sulfur cluster assembly
Biological Processnuclear polyadenylation-dependent antisense transcript catabolic process
Biological Processnuclear polyadenylation-dependent CUT catabolic process
Biological Processnuclear polyadenylation-dependent rRNA catabolic process
Biological Processnuclear polyadenylation-dependent snoRNA catabolic process
Biological Processnuclear polyadenylation-dependent snRNA catabolic process
Biological Processpoly(A)-dependent snoRNA 3'-end processing
Biological ProcessTRAMP-dependent tRNA surveillance pathway

Keywords

Names & Taxonomy

Protein names

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

Gene names

    • ORF names
      Mgra_00008943

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • VN-18
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Tylenchomorpha > Tylenchoidea > Meloidogynidae > Meloidogyninae > Meloidogyne

Accessions

  • Primary accession
    A0A8S9ZEE4

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane27-45Helical

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for coiled coil, region, motif, domain.

Type
IDPosition(s)Description
Coiled coil51-169
Region208-227Disordered
Motif422-425Cx2C motif 1
Region422-436Fe-S binding site B
Motif433-436Cx2C motif 2
Domain589-7513'-5' exonuclease

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.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    758
  • Mass (Da)
    85,621
  • Last updated
    2022-10-12 v1
  • Checksum
    A3A261A1B90E0822
MAESSQNYRRLGRNGHSLSYCSKSSSAFFLLISFAFVFSLVYLYFSTNSELQSFRTDFESLNSKNLNLKNELLRANIKIEELTKAESECKSSKNELDARFQVCKRDLYDKNTSLGRIETNRADCENVLRDLKSKFETVNSALKESVSEKQSQASIIANLTRTIDQLRNQLALGSSVGILPSGKSADLNHEGIAHRFIETGPKNITLKADKKESPREQIMAPSKDDLVAKDDAANEKQSGDAPKLLPGGRVHLAEQEEKREQLSNHKELLHAAANLDKQQEVFDDVVAEKEYKNENGIENMENKAIANKLTTTKSEKSLFMELLLNLLLQITMDQAIKMSSSDKPTQDSTSTKIMEKDPAVDDLIDEDSLLEPKDLERPAQKACEAVVEQKKKRACKNCTCGLAELEDIEDEKSELPPLKSSCGNCYLGDAFRCSTCPYLGTPPFEKDEQGKVMLSKLMDRLLLLSDNLVQQLKDIPPEYIGNEIIDRLIRIFNKFSLTISVKDGNVSGGQFQLICGPLIGKIDNLYAQVDSELSKDAEENQKIIEAEASCQHKQKSKKRKLFLPDLLPTQVPDPLPVEISLKRTPFHFLNLPQSVIDLGRVLKSVGVFAFDLERTVPFRHGRTSKVCLLQISTQNEDFVIDTLAYGMKNAVTNYLKTAFEDPQIIKIVHGHDDTKWLRTAFDIFISNHFDTSSTGYNLQQLVYVACGIKLEKIYQTADWMHRPLSKNMLEYARLDTHYLISCWGYLTKTSRRDFFSHS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABEBT010000130
EMBL· GenBank· DDBJ
KAF7630784.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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