G7N8B1 · G7N8B1_MACMU
- ProteinMethionine aminopeptidase
- GeneMETAP1D
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids335 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
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 | 161 | substrate | |||
Binding site | 178 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 189 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 189 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 252 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 259 | substrate | |||
Binding site | 284 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 315 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 315 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMethionine aminopeptidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionG7N8B1
- Secondary accessions
Proteomes
Organism-specific databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 97-321 | Peptidase M24 | |||
Sequence similarities
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length335
- Mass (Da)37,143
- Last updated2012-01-25 v1
- MD5 ChecksumB694AF73C1ACFA62E056B5C4C8450B5C
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F7F2S1 | F7F2S1_MACMU | METAP1D | 331 | ||
A0A1D5Q0E4 | A0A1D5Q0E4_MACMU | METAP1D | 351 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JU333797 EMBL· GenBank· DDBJ | AFE77552.1 EMBL· GenBank· DDBJ | mRNA | ||
JV046650 EMBL· GenBank· DDBJ | AFI36721.1 EMBL· GenBank· DDBJ | mRNA |