A0A024SFM4 · A0A024SFM4_HYPJR

Function

Catalytic activity

  • Hydrolyzes the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids with aliphatic side chains and P3' is any C-terminal residue.
    EC:3.4.24.84 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

1852100200300400500600700800
Type
IDPosition(s)Description
Binding site691Zn2+ (UniProtKB | ChEBI); catalytic
Active site692
Binding site695Zn2+ (UniProtKB | ChEBI); catalytic
Binding site770Zn2+ (UniProtKB | ChEBI); catalytic
Active site774Proton donor

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Molecular Functionsyntaxin binding
Biological ProcessCAAX-box protein processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ste24 endopeptidase
  • EC number

Gene names

    • ORF names
      M419DRAFT_129141

Organism names

Accessions

  • Primary accession
    A0A024SFM4

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane565-583Helical
Transmembrane589-611Helical

Keywords

  • Cellular component

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region38-84Disordered
Compositional bias51-84Basic and acidic residues
Region315-391Disordered
Compositional bias352-379Acidic residues
Domain434-618CAAX prenyl protease 1 N-terminal
Domain621-825Peptidase M48
Region832-852Disordered

Sequence similarities

Belongs to the taxilin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    852
  • Mass (Da)
    98,377
  • Last updated
    2014-07-09 v1
  • Checksum
    AF044668C3728F59
MDSTEASRLLQARISQLEQDAAGEKDQEMEIEREVKRANRDLLQQRSSELLADMRRLERENQKNKKRGDALQKERDASRTELSKTVGLKEKLEKLCRELQRDNNKMKNENKELQSTQKRNNTAWDEKFASLLSKLEGYQEEKDTPKKQVVDMEMDELFRVRFKSFIEQYELRELHFHSLMRTKELEVQYHLSRHDREKKNAEAEATKARHLQAQVHAFTKTETELRNQLNVYVDKFKQVEDTLNNSNDLFLSFRKEMEDMSKKGKRLEKENEALKRQKEATTANIIHMAEERQEWKKKIEAAEKKNEKLMSIIQQMQQQGRKVPPAAASTVEACYPESQGPAVVESRGEGEGEDSEYSDEEGEEEGLSEFDDDTEEEPQPSEQSAPVPHRNTATMDFLQRLSQFLDRPLFPWKRLILGFSVGQFLFESLLTFRQYRVLQSPKPPAVLAKEVSQETFDKSQAYGRAKARFSVASGLWGQIANFAFIQLDVMPKLWSWTGDLLLRYAPARFTGEISHSIVFVFAFMLIQQGLSLPTRIYSTFVLEEKFGFNKQTPGLFISDMVKTNLLTAVLMPPILAGFLKIIQKTGSQFVFYTWVFTAGIQLLMTTLYPTFIQPLFNKLSPLEDGELKTKVNELAARFKFPLHELYVIDGSKRSAHSNAFFYGLPWKKHIVIYDTLLEKSEPEEVLAILAHELGHWKLGHTTSLFGISQAHLLYIFSLFSVFINNRSLYASFGFHNERPIIIGFLLFSDALSPMDTVIQFLLHIVSRTFEFQADAFANSLGMRAELATSLIKLHVQNLSSMDADWMYASYHFSHPHLSERLKALDWKGEQAVTSEKEKEQEGVVKATGRDEL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias51-84Basic and acidic residues
Compositional bias352-379Acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KI911144
EMBL· GenBank· DDBJ
ETS02977.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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