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 |