A0AA43QK86 · A0AA43QK86_9LECA
- ProteinMethionine aminopeptidase 2
- GeneMAP2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids426 (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
Protein has several cofactor binding sites:
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 | 188 | substrate | |||
Binding site | 208 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 219 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 219 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 288 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 296 | substrate | |||
Binding site | 321 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 416 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 416 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | initiator methionyl aminopeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metalloaminopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMethionine aminopeptidase 2
- EC number
- Short namesMAP 2 ; MetAP 2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Lecanoromycetes > OSLEUM clade > Lecanoromycetidae > Lecanorales > Lecanorineae > Ramalinaceae > Ramalina
Accessions
- Primary accessionA0AA43QK86
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-84 | Disordered | |||
Compositional bias | 8-33 | Polar residues | |||
Compositional bias | 50-66 | Basic residues | |||
Domain | 119-322 | Peptidase M24 | |||
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length426
- Mass (Da)46,654
- Last updated2024-01-24 v1
- Checksum69633184508FBE6D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 8-33 | Polar residues | |||
Compositional bias | 50-66 | Basic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAPUFD010000005 EMBL· GenBank· DDBJ | MDI1487252.1 EMBL· GenBank· DDBJ | Genomic DNA |