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Annotation rule MF_03174
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General rule information [?]

Accession MF_03174
Dates 31-MAY-2013 (Created)
20-NOV-2019 (Last updated, Version 6)
Name MetAP_1_euk
Scope
Eukaryota
Templates P53582 (MAP11_HUMAN); Q01662 (MAP1_YEAST); P0AE18 (MAP1_ECOLI): [Recover all]
case <OC:Eukaryota>
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

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 [?]

case <FTTag:Ribo>
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;
Cofactor Co(2+)
Zn(2+)
Mn(2+)
Fe(2+)
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.
case <FTTag:Ribo>
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 [?]

case <FTTag:Ribo>
end case

Gene Ontology [?]

case <FTTag:Ribo>
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:0070084; Biological process: protein initiator methionine removal.

Cross-references [?]

Pfam PF00557; Peptidase_M24; 1;
PRINTS PR00599; MAPEPTIDASE; 1;
TIGRFAMs TIGR00500; met_pdase_I; 1;
PROSITE PS00680; MAP_1; 1;

Computed features [?]

case not <FTTag:Ribo>
General TransitM; -; 0-1; trigger=yes;
end case
case <OC:Viridiplantae> and not (<FTTag:Ribo> or <AnyFeature:TransitM>)
General TransitC; -; 0-1; trigger=yes;
end case

Features [?]

From: MAP11_HUMAN (P53582)
Key     From     To       Description   Tag   Condition   FTGroup
METAL     220     220       Divalent metal cation 1     D   1
METAL     231     231       Divalent metal cation 1     D   1
METAL     231     231       Divalent metal cation 2; catalytic     D   1
METAL     294     294       Divalent metal cation 2; catalytic; via tele nitrogen     H   1
METAL     327     327       Divalent metal cation 2; catalytic     E   1
METAL     358     358       Divalent metal cation 1     E   1
METAL     358     358       Divalent metal cation 2; catalytic     E   1
BINDING     203     203       Substrate     H  
BINDING     301     301       Substrate     H  
From: MAP1_YEAST (Q01662)
REGION     22     66       Zinc finger-like; important for proper ribosome association   Ribo   C-x(2,4)-C-x(7,9)-C-x(2)-C-x(9,12)-C-x(3)-C-x(7)-H-x(3)-H  

Additional information [?]

Size range 335-404 amino acids
Related rules None
Fusion None