STRINGSTRING
ATEG_10326 ATEG_10326 ATEG_10186 ATEG_10186 ATEG_10146 ATEG_10146 ATEG_10115 ATEG_10115 ATEG_09990 ATEG_09990 ATEG_09137 ATEG_09137 ATEG_08990 ATEG_08990 ATEG_08717 ATEG_08717 ATEG_08660 ATEG_08660 ampp ampp ATEG_08013 ATEG_08013 ATEG_07980 ATEG_07980 ATEG_07766 ATEG_07766 ATEG_07578 ATEG_07578 pepP pepP ATEG_06810 ATEG_06810 ATEG_06681 ATEG_06681 ATEG_05540 ATEG_05540 ATEG_05313 ATEG_05313 ATEG_05031 ATEG_05031 ATEG_05010 ATEG_05010 ATEG_04884 ATEG_04884 ATEG_04374 ATEG_04374 ATEG_03836 ATEG_03836 ATEG_03700 ATEG_03700 ataJ ataJ ATEG_03030 ATEG_03030 ATEG_02309 ATEG_02309 ATEG_00976 ATEG_00976 ATEG_00858 ATEG_00858 ATEG_00426 ATEG_00426
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
ATEG_10326Peptidase_M14 domain-containing protein. (540 aa)
ATEG_10186Uncharacterized protein. (572 aa)
ATEG_10146Methionine 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_10115Peptide hydrolase; Belongs to the peptidase M28 family. (772 aa)
ATEG_09990Peptide hydrolase; Belongs to the peptidase M28 family. (503 aa)
ATEG_09137Peptide hydrolase; Belongs to the peptidase M28 family. (505 aa)
ATEG_08990M20_dimer domain-containing protein. (477 aa)
ATEG_08717M20_dimer domain-containing protein. (568 aa)
ATEG_08660Uncharacterized protein. (580 aa)
amppProbable Xaa-Pro aminopeptidase P; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. (654 aa)
ATEG_08013Uncharacterized protein. (991 aa)
ATEG_07980Aminopeptidase. (884 aa)
ATEG_07766Uncharacterized protein. (652 aa)
ATEG_07578Uncharacterized protein. (561 aa)
pepPProbable Xaa-Pro aminopeptidase pepP; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. (466 aa)
ATEG_06810Uncharacterized protein. (1176 aa)
ATEG_06681AMP_N domain-containing protein. (499 aa)
ATEG_05540Methionine 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_05313Aminopeptidase. (882 aa)
ATEG_050311,3-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_05010Dipeptidase; Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family. (433 aa)
ATEG_04884Uncharacterized protein. (225 aa)
ATEG_04374Uncharacterized protein. (521 aa)
ATEG_03836Uncharacterized protein. (783 aa)
ATEG_03700Methionine 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)
ataJDipeptidase 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_03030Peptide hydrolase; Belongs to the peptidase M28 family. (1432 aa)
ATEG_02309M20_dimer domain-containing protein. (574 aa)
ATEG_00976Uncharacterized protein. (428 aa)
ATEG_00858Probable Xaa-Pro aminopeptidase ATEG_00858; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. (488 aa)
ATEG_00426Methionine 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)
Your Current Organism:
Aspergillus terreus
NCBI taxonomy Id: 341663
Other names: A. terreus NIH2624, Aspergillus terreus FGSC A1156, Aspergillus terreus NIH2624
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