A0A0M9ERR0 · A0A0M9ERR0_FUSLA
- ProteinMethionine aminopeptidase 2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids441 (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 | 194 | substrate | ||||
Sequence: H | ||||||
Binding site | 214 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 225 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 225 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 294 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 302 | substrate | ||||
Sequence: H | ||||||
Binding site | 327 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 422 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 422 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E |
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 > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium
Accessions
- Primary accessionA0A0M9ERR0
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-97 | Disordered | ||||
Sequence: MAAQVPTEALKELNVADGSQKPGANAQSNTDAAGDEHGGDDSEDEADGVAPAEGAAKKKKKRKPKKKKKNPTSQSDPPRVQVSQLFPNKSYPPGEEV | ||||||
Compositional bias | 74-88 | Polar residues | ||||
Sequence: QSDPPRVQVSQLFPN | ||||||
Domain | 126-336 | Peptidase M24 | ||||
Sequence: YREAAEIHRQVRQWTQKNVKPGQTLTSIAEGIEDGVRALTGHSGLEEGDSLKAGMGFPCGLSLNHCAAHYTPNAGNKMVLQKEDVMKVDFGVHVNGRIVDSAFTMSFDNKYDNLLQAVKEATNAGIREAGIDARVGEIGGVIQETMESFEVEIDGTTYPVKSIRNLTGHNILPYSIHGTKAVPIVKSNDQTKMEEGDVFAIETFGSTGNGY |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length441
- Mass (Da)48,348
- Last updated2015-12-09 v1
- ChecksumAC4E4916F1234E87
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 74-88 | Polar residues | ||||
Sequence: QSDPPRVQVSQLFPN |
Keywords
- Technical term