A0A125S6H1 · A0A125S6H1_9FUNG
- ProteinMethionine aminopeptidase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids352 (go to sequence)
- Protein existenceEvidence at transcript level
- 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.
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
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 zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 183 | N-terminal L-methionine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 200 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 211 | Zn2+ 4 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 211 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 274 | Zn2+ 4 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 281 | N-terminal L-methionine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 307 | Zn2+ 4 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 338 | Zn2+ 4 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 338 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosolic ribosome | |
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
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Mucoromycetes > Mucorales > Mucorineae > Mucoraceae > Actinomucor
Accessions
- Primary accessionA0A125S6H1
Subcellular Location
Interaction
Subunit
Associates with the 60S ribosomal subunit of the 80S translational complex.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-58 | C6H2-type | ||||
Sequence: KPLCASIECKNKAHLQCPTCVKLGKNGESFFCSQDCFKKSWGSHKAVHGDTKSPY |
Sequence similarities
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length352
- Mass (Da)38,978
- Last updated2016-04-13 v1
- Checksum796F3C95E8BF159C