D8PR70 · MAP2_SCHCM
- ProteinMethionine aminopeptidase 2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids423 (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 | 176 | substrate | ||||
Sequence: H | ||||||
Binding site | 196 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 207 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 207 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 276 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 284 | substrate | ||||
Sequence: H | ||||||
Binding site | 309 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 404 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 404 | 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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Schizophyllaceae > Schizophyllum
Accessions
- Primary accessionD8PR70
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000407667 | 1-423 | Methionine aminopeptidase 2 | |||
Sequence: MTDVIDAKPEEAKKVPPEVEDEDSGDESAPEASAAGGEATKKKKKKKKPKKKKKAAEQSEPPRVGLSKLFPNGIYPEGEIQPYKDDNAYRTTSEEKRYLERITCEDPDETYQNIRKGAEVHRQVRQYAQRTIKPGMTMTEIANLIEDGTRALVEENGLEAGIGFPTGLSLNNCAAHYTPNAGDTIVLQQGDVMKVDIGVQVKGRIVDSAFTMTFEPTYDKLLEAVRAATNTGIREAGIDARLGEIAGAIQETMESYEVEVNGKLIPVKPIANLSGHSIDRYTIHAGKSVCLVKNDDQTKMEEGEYFAIETFGSTGRGRVVDGGECSHYARKVDAPHVPLRLTTAKSLLKSINKNFGTIPFCRRYLDRIGESKYLLALNHLVQQGIVEDYPPLYDQQGSMTAQFEHTILLRPTVKEVVSRGDDY |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-20 | Basic and acidic residues | ||||
Sequence: MTDVIDAKPEEAKKVPPEVE | ||||||
Region | 1-89 | Disordered | ||||
Sequence: MTDVIDAKPEEAKKVPPEVEDEDSGDESAPEASAAGGEATKKKKKKKKPKKKKKAAEQSEPPRVGLSKLFPNGIYPEGEIQPYKDDNAY |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length423
- Mass (Da)46,783
- Last updated2010-10-05 v1
- Checksum3680863E582C4A34
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-20 | Basic and acidic residues | ||||
Sequence: MTDVIDAKPEEAKKVPPEVE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL377302 EMBL· GenBank· DDBJ | EFJ03808.1 EMBL· GenBank· DDBJ | Genomic DNA |