| Analysis | rpsblast_cdd | Start | 2 |
| End | 217 | Strand | + |
| Length | 216 | Note | Gaps:10 |
| Hit Coverage | 35.25 | Hit Length | 590 |
| Hit Pident | 37.02 | E Val | 1e-55 |
| Hit Description | cd09605 M3A Peptidase M3A family includes Thimet oligopeptidase dipeptidyl carboxypeptidase and mitochondrial intermediate peptidase. The peptidase M3-like family also called neurolysin-like family is part of the "zincins" metallopeptidases and includes M3 M2 and M32 families of metallopeptidases. The M3 family is subdivided into two subfamilies: the widespread M3A which comprises a number of high-molecular mass endo- and exopeptidases from bacteria archaea protozoa fungi plants and animals and the small M3B whose members are enzymes primarily from bacteria. Well-known mammalian/eukaryotic M3A endopeptidases are the thimet oligopeptidase (TOP endopeptidase 3.4.24.15) neurolysin (alias endopeptidase 3.4.24.16) and the mitochondrial intermediate peptidase. The first two are intracellular oligopeptidases which act only on relatively short substrates of less than 20 amino acid residues while the latter cleaves N-terminal octapeptides from proteins during their import into the mitochondria. The M3A subfamily also contains several bacterial endopeptidases collectively called oligopeptidases A as well as a large number of bacterial carboxypeptidases called dipeptidyl peptidases (Dcp Dcp II peptidyl dipeptidase EC 3.4.15.5). The peptidases in the M3 family contain the HEXXH motif that forms the active site in conjunction with a C-terminally-located Glutamic acid (Glu) residue. A single zinc ion is ligated by the side-chains of the two Histidine (His) residues and the more C-terminal Glu. Most of the peptidases are synthesized without signal peptides or propeptides and function intracellularly. The structure of neurolysin shows similarities to those of angiotensin-converting enzyme (ACE peptidyl-dipeptidase A) peptidase unit 2 belonging to peptidase family M2. ACE is an enzyme responsible for cleavage of dipeptides from the C-termini of proteins notably converting angiotensin I to angiotensin II in mammals. There are similarities to the thermostable carboxypeptidases from Pyrococcus furiosus carboxypeptidase (PfuCP) and Thermus aquaticus (TaqCP) belonging to peptidase family M32. Little is known about function of this family including carboxypeptidases Taq and Pfu. | Hit Pcons | 16.83 |
| Name | Qrob_P0660200.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0660200.2 | Quercus robur | 0.0 | egn | (M=2) 3.4.24.70 - Oligopeptidase A. | EC:3.4.24.70 | validated |
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