A0A125S6H1 · A0A125S6H1_9FUNG

  • Protein
    Methionine aminopeptidase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

function

Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).

Catalytic activity

  • Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
    EC:3.4.11.18 (UniProtKB | ENZYME | Rhea)

Cofactor

Protein has several cofactor binding sites:
Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site183N-terminal L-methionine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site200Zn2+ 3 (UniProtKB | ChEBI)
Binding site211Zn2+ 4 (UniProtKB | ChEBI); catalytic
Binding site211Zn2+ 3 (UniProtKB | ChEBI)
Binding site274Zn2+ 4 (UniProtKB | ChEBI); catalytic
Binding site281N-terminal L-methionine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site307Zn2+ 4 (UniProtKB | ChEBI); catalytic
Binding site338Zn2+ 4 (UniProtKB | ChEBI); catalytic
Binding site338Zn2+ 3 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosolic ribosome
Molecular Functioninitiator methionyl aminopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloaminopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Methionine aminopeptidase
  • EC number

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Mucoromycetes > Mucorales > Mucorineae > Mucoraceae > Actinomucor

Accessions

  • Primary accession
    A0A125S6H1

Subcellular Location

Keywords

Interaction

Subunit

Associates with the 60S ribosomal subunit of the 80S translational complex.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-58C6H2-type

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    352
  • Mass (Da)
    38,978
  • Last updated
    2016-04-13 v1
  • Checksum
    796F3C95E8BF159C
MLEKPLCASIECKNKAHLQCPTCVKLGKNGESFFCSQDCFKKSWGSHKAVHGDTKSPYDPFKTFKYAGPLRAVYPLSPRRTVPEEISRPDYAESGISRSELMSRGSDIKVLTPEEIEGAKKACAITREVLELAAKSIRVGMTTDELDRIVHEATIERGAYPSPLNYNYFPKSCCTSLNEVICHGIPDQRPLADGDILNIDISCFYQGFHGDTNGTYLVGNVDEAGQKLVNVTRECLEKAIAAVKPGMRYRDFGKIIEDHATKNGFSVVRAFVGHGIHQLFHCAPNVPHYANNKAIGVCKPGHIFTIEPMICEGVHQELMWPDGWTATTKDGKRSAQFEHTLLVTETGVEILT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KP973584
EMBL· GenBank· DDBJ
AME15507.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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