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Annotation rule MF_03174 |
General rule information
[?]
Accession |
MF_03174 |
Dates |
31-MAY-2013 (Created) 20-NOV-2019 (Last updated, Version 6) |
case <OC:Eukaryota>
end case
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <AnyFeature:TransitM>
Protein name |
RecName:
|
Full=Methionine aminopeptidase 1, mitochondrial;
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Short=MAP 1;
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Short=MetAP 1;
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EC 3.4.11.18;
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AltName:
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Full=Peptidase M 1;
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else case <AnyFeature:TransitC>
Protein name |
RecName:
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Full=Methionine aminopeptidase 1, chloroplastic;
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Short=MAP 1;
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Short=MetAP 1;
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EC 3.4.11.18;
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AltName:
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Full=Peptidase M 1;
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else
Protein name |
RecName:
|
Full=Methionine aminopeptidase 1;
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Short=MAP 1;
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Short=MetAP 1;
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EC 3.4.11.18;
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AltName:
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Full=Peptidase M 1;
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|
end case
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. |
case <FTTag:Ribo>
end case
case <FTTag:Ribo>
GO:0022626; Cellular component: cytosolic ribosome.
else case <AnyFeature:TransitM>
else case <AnyFeature:TransitC>
end case
GO:0046872; Molecular function: metal ion binding.
GO:0070006; Molecular function: metalloaminopeptidase activity.
GO:0070084; Biological process: protein initiator methionine removal.
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
From: MAP11_HUMAN (P53582) |
Key
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From
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To
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Description
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Tag
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Condition
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|
FTGroup
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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
|
|
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BINDING
|
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301
|
|
301
|
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Substrate
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H
|
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From: MAP1_YEAST (Q01662) |
REGION
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22
|
|
66
|
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Zinc finger-like; important for proper ribosome association
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Ribo
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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
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Additional information
[?]
Size range |
335-404 amino acids |
Related rules |
None |
Fusion |
None |