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ATEG_10326 | Peptidase_M14 domain-containing protein. (540 aa) | ||||
ATEG_10186 | Uncharacterized protein. (572 aa) | ||||
ATEG_10146 | Methionine aminopeptidase 2-1; 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); Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily. (453 aa) | ||||
ATEG_10115 | Peptide hydrolase; Belongs to the peptidase M28 family. (772 aa) | ||||
ATEG_09990 | Peptide hydrolase; Belongs to the peptidase M28 family. (503 aa) | ||||
ATEG_09137 | Peptide hydrolase; Belongs to the peptidase M28 family. (505 aa) | ||||
ATEG_08990 | M20_dimer domain-containing protein. (477 aa) | ||||
ATEG_08717 | M20_dimer domain-containing protein. (568 aa) | ||||
ATEG_08660 | Uncharacterized protein. (580 aa) | ||||
ampp | Probable Xaa-Pro aminopeptidase P; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. (654 aa) | ||||
ATEG_08013 | Uncharacterized protein. (991 aa) | ||||
ATEG_07980 | Aminopeptidase. (884 aa) | ||||
ATEG_07766 | Uncharacterized protein. (652 aa) | ||||
ATEG_07578 | Uncharacterized protein. (561 aa) | ||||
pepP | Probable Xaa-Pro aminopeptidase pepP; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. (466 aa) | ||||
ATEG_06810 | Uncharacterized protein. (1176 aa) | ||||
ATEG_06681 | AMP_N domain-containing protein. (499 aa) | ||||
ATEG_05540 | Methionine aminopeptidase 2-2; 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); Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily. (445 aa) | ||||
ATEG_05313 | Aminopeptidase. (882 aa) | ||||
ATEG_05031 | 1,3-beta-glucanosyltransferase; Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall; Belongs to the glycosyl hydrolase 72 family. (467 aa) | ||||
ATEG_05010 | Dipeptidase; Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family. (433 aa) | ||||
ATEG_04884 | Uncharacterized protein. (225 aa) | ||||
ATEG_04374 | Uncharacterized protein. (521 aa) | ||||
ATEG_03836 | Uncharacterized protein. (783 aa) | ||||
ATEG_03700 | Methionine aminopeptidase; 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). (400 aa) | ||||
ataJ | Dipeptidase ataJ; Dipeptidase; part of the gene cluster that mediates the biosynthesis of acetylaranotin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide-bridged cyclic dipeptide. The first step of acetylaranotin biosynthesis is performed by the NRPS ataP which produces diketopiperazine cyclo-L-Phe-L-Phe via the condensation of 2 phenylalanines (L-Phe). The ataC domain of ataTC then catalyzes the formation of bishydroxylation of cyclo-L-Phe-L-Phe. The glutathione S-transferase domain ataG in ataIMG further catalyzes the conjugation of two g [...] (410 aa) | ||||
ATEG_03030 | Peptide hydrolase; Belongs to the peptidase M28 family. (1432 aa) | ||||
ATEG_02309 | M20_dimer domain-containing protein. (574 aa) | ||||
ATEG_00976 | Uncharacterized protein. (428 aa) | ||||
ATEG_00858 | Probable Xaa-Pro aminopeptidase ATEG_00858; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. (488 aa) | ||||
ATEG_00426 | Methionine aminopeptidase; 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). (345 aa) |