| Accession | TIGR00501 |
| Name | met_pdase_II |
| Function | methionine aminopeptidase, type II |
| Gene Symbol | map |
| Trusted Cutoff | 222.65 |
| Domain Trusted Cutoff | 222.65 |
| Noise Cutoff | 184.60 |
| Domain Noise Cutoff | 184.60 |
| Isology Type | equivalog |
| EC Number | 3.4.11.18 |
| HMM Length | 295 |
| Mainrole Category | Protein fate |
| Subrole Category | Protein modification and repair |
| Gene Ontology Term | GO:0004239: methionyl aminopeptidase activity molecular_function |
| | GO:0006464: protein modification process biological_process |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:08PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Methionine aminopeptidase (map) is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. The role of this protein in general is to produce the mature amino end of cytosolic proteins by removing the N-terminal methionine. This model describes type II, among which the eukaryotic members typically have an N-terminal extension not present in archaeal members. It can act cotranslationally. The enzyme from rat has been shown to associate with translation initiation factor 2 (IF-2) and may have a role in translational regulation. |
| References | A2 hmmalign
RM Medline; 98060511;
RM Medline; 95372350;
SE TIGR
AL clustalw
BD 0551 |
