Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR002467 is a Peptidase M24A, methionine aminopeptidase, subfamily 1.
<p>This group of metallopeptidases belong to MEROPS peptidase family M24 (clan MG), subfamily M24A.</p> <p>Methionine aminopeptidase ([ec:3.4.11.18]) (MAP) catalyses the hydrolytic cleavage of the N-terminal methionine from newly synthesised polypeptides if the penultimate amino acid is small, with different tolerance to Val and Thr at this position [[cite:PUB00070140]]. All MAP studied to date are monomeric proteins that require cobalt ions for activity. Two subfamilies of MAP enzymes are known to exist [[cite:PUB00004871], [cite:PUB00005454]]. While being evolutionary related, they only share a limited amount of sequence similarity, mostly clustered around the residues shown to be involved in cobalt-binding in Escherichia coli MAP [[cite:PUB00000379]]. Subfamily 1 consists of enzymes from prokaryotes as well as eukaryotic MAP-1, while the second group ([interpro:IPR002468]) is made up of archaeal MAP and eukaryotic MAP-2.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Aminopeptidase activity | Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain. | ||
| Biological process | Proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. | ||
| Molecular function | Metalloexopeptidase activity | Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: methionine aminopeptidase 1A-like [Cicer arietinum] gi|502168167|ref|XP_004514335.1| | 16 | ||
| – | PREDICTED: methionine aminopeptidase 1A-like [Cicer arietinum] gi|502168167|ref|XP_004514335.1| | 15 | ||
| – | PREDICTED: methionine aminopeptidase 1D, chloroplastic/mitochondrial-like [Glycine max] gi|356496878|ref|XP_003517292.1| | 13 | ||
| – | Methionine aminopeptidase; TAIR: AT1G13270.1 methionine aminopeptidase 1B; Swiss-Prot: sp|Q9FV52|MAP1B_ARATH Methionine aminopeptidase 1B, chloroplastic; TrEMBL-Plants: tr|I1JDW6|I1JDW6_SOYBN Methionine aminopeptidase; Found in the gene: LotjaGi2g1v0281000 | 20 | ||
| – | Methionine aminopeptidase; TAIR: AT4G37040.1 methionine aminopeptidase 1D; Swiss-Prot: sp|Q9FV50|MAP1D_ARATH Methionine aminopeptidase 1D, chloroplastic/mitochondrial; TrEMBL-Plants: tr|A0A0R0LM01|A0A0R0LM01_SOYBN Methionine aminopeptidase; Found in the gene: LotjaGi2g1v0400100 | 14 | ||
| – | Methionine aminopeptidase; TAIR: AT4G37040.1 methionine aminopeptidase 1D; Swiss-Prot: sp|Q9FV50|MAP1D_ARATH Methionine aminopeptidase 1D, chloroplastic/mitochondrial; TrEMBL-Plants: tr|A0A0R0LM01|A0A0R0LM01_SOYBN Methionine aminopeptidase; Found in the gene: LotjaGi2g1v0400100 | 14 | ||
| – | Methionine aminopeptidase; TAIR: AT2G45240.1 methionine aminopeptidase 1A; Swiss-Prot: sp|Q9SLN5|MAP1A_ARATH Methionine aminopeptidase 1A; TrEMBL-Plants: tr|V7AMJ4|V7AMJ4_PHAVU Methionine aminopeptidase; Found in the gene: LotjaGi3g1v0436800 | 18 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd01086 | CDD | 1 | 14.29 |