HAMAP rule MF_03174
General rule information
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Accession | MF_03174 |
Dates | 31-MAY-2013 (Created)
1-JUN-2023 (Last updated, Version 11) |
Name | MetAP_1_euk |
Scope(s) |
Eukaryota |
Template(s) | P53582 (MAP11_HUMAN); Q01662 (MAP1_YEAST); P0AE18 (MAP1_ECOLI); [ Recover all ] |
Triggered by |
case c? <OC:Eukaryota>
HAMAP; MF_01974 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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Identifier | MAP1 |
case <AnyFeature:TransitM> | |
Protein name | RecName: Full=Methionine aminopeptidase 1, mitochondrial; Short=MAP 1; Short=MetAP 1; EC=3.4.11.18; AltName: Full=Peptidase M 1; |
else case <AnyFeature:TransitC> | |
Protein name | RecName: Full=Methionine aminopeptidase 1, chloroplastic; Short=MAP 1; Short=MetAP 1; EC=3.4.11.18; AltName: Full=Peptidase M 1; |
else | |
Protein name | RecName: Full=Methionine aminopeptidase 1; Short=MAP 1; Short=MetAP 1; EC=3.4.11.18; AltName: Full=Peptidase M 1; |
end case |
Comments
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case <AnyFeature:PS52013> | |
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). |
else case <AnyFeature:TransitM> or <AnyFeature:TransitC> | |
FUNCTION | 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. |
else | |
FUNCTION | 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). |
end case | |
CATALYTIC ACTIVITY | Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; |
case <AnyFeature:PS52013> | |
COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Fe(2+); Xref=ChEBI: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. |
else | |
COFACTOR | Name=Co(2+); Xref=ChEBI:CHEBI:48828; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Fe(2+); Xref=ChEBI: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 Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. |
end case | |
case <AnyFeature:PS52013> | |
SUBUNIT | Associates with the 60S ribosomal subunit of the 80S translational complex. |
SUBCELLULAR LOCATION | Cytoplasm. |
end case | |
SIMILARITY | Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. |
Keywords
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Aminopeptidase | |
Hydrolase | |
Protease | |
Metal-binding | |
case <AnyFeature:PS52013> | |
Cytoplasm | |
end case |
Gene Ontology
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case <AnyFeature:PS52013> | |
GO:0022626; Cellular component:cytosolic ribosome | |
else case <AnyFeature:TransitM> | |
GO:0005739; Cellular component:mitochondrion | |
else case <AnyFeature:TransitC> | |
GO:0009507; Cellular component:chloroplast | |
end case | |
GO:0046872; Molecular function:metal ion binding | |
GO:0070006; Molecular function:metalloaminopeptidase activity | |
GO:0004239; Molecular function:initiator methionyl aminopeptidase activity |
Cross-references
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Pfam | PF00557; Peptidase_M24; 1; |
PRINTS | PR00599; MAPEPTIDASE; 1; |
NCBIfam | TIGR00500; met_pdase_I; 1; |
PROSITE | PS00680; MAP_1; 1; |
PROSITE | PS52013; ZF_C6H2; 0-1; |
General | TransitM; -; 0-1; |
General | TransitC; -; 0-1; |
Features
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case <AnyFeature:PS52013> | ||||||||||||
From: MAP11_HUMAN (P53582) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 203 | 203 | /ligand="a protein" /ligand_id="ChEBI:CHEBI:16541" /ligand_part="N-terminal L-methionine residue" /ligand_part_id="ChEBI:CHEBI:64731" |
H | ||||||||
BINDING | 220 | 220 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
D | ||||||||
BINDING | 231 | 231 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
D | ||||||||
BINDING | 231 | 231 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4" /ligand_note="catalytic" |
D | ||||||||
BINDING | 294 | 294 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4" /ligand_note="catalytic" |
H | ||||||||
BINDING | 301 | 301 | /ligand="a protein" /ligand_id="ChEBI:CHEBI:16541" /ligand_part="N-terminal L-methionine residue" /ligand_part_id="ChEBI:CHEBI:64731" |
H | ||||||||
BINDING | 327 | 327 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4" /ligand_note="catalytic" |
E | ||||||||
BINDING | 358 | 358 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
E | ||||||||
BINDING | 358 | 358 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4" /ligand_note="catalytic" |
E | ||||||||
else | ||||||||||||
From: MAP12_HUMAN (Q6UB28) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 161 | 161 | /ligand="substrate" | H | ||||||||
BINDING | 178 | 178 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
D | ||||||||
BINDING | 189 | 189 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
D | ||||||||
BINDING | 189 | 189 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic" |
D | ||||||||
BINDING | 252 | 252 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic" |
H | ||||||||
BINDING | 259 | 259 | /ligand="substrate" | H | ||||||||
BINDING | 284 | 284 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic" |
E | ||||||||
BINDING | 315 | 315 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
E | ||||||||
BINDING | 315 | 315 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic" |
E | ||||||||
end case |
Additional information
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Size range | 335-404 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |