A0A0D1E3G9 · A0A0D1E3G9_USTMA
- ProteinMethionine aminopeptidase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids387 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
Cofactor
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. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 144 | substrate | |||
Binding site | 161 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 172 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 172 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 238 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 245 | substrate | |||
Binding site | 271 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 303 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 303 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | cytosolic ribosome | |
Molecular Function | initiator methionyl aminopeptidase activity | |
Molecular Function | metalloaminopeptidase activity | |
Molecular Function | mRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | negative regulation of gene expression | |
Biological Process | protein processing |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMethionine aminopeptidase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Mycosarcoma
Accessions
- Primary accessionA0A0D1E3G9
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 79-310 | Peptidase M24 | |||
Region | 340-387 | Disordered | |||
Compositional bias | 354-378 | Polar residues | |||
Sequence similarities
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length387
- Mass (Da)42,003
- Last updated2015-04-29 v1
- MD5 Checksum45F56B5AB347602E2597DF3FDD66F499
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 354-378 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM003142 EMBL· GenBank· DDBJ | KIS70659.1 EMBL· GenBank· DDBJ | Genomic DNA |