P1 family peptidase such as DmpA aminopeptidase that self-activates to produce a two-chain form in which the new N-terminus is the serine that is the nucleophile in the self-cleaving reaction
L-Aminopeptidase D-amidase/D-esterase (DmpA) family; DmpA catalyzes the release of N-terminal ...
13-341
1.06e-154
L-Aminopeptidase D-amidase/D-esterase (DmpA) family; DmpA catalyzes the release of N-terminal D and L amino acids from peptide susbtrates. DmpA is synthesized as a single polypeptide precursor, which is autocatalytically cleaved to the active heterodimeric form. The cleavage results in two polypeptide chains, with one chain containing an N-terminal nucleophile. This group represents one of the rare aminopeptidases that are not metalloenzymes. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine.
:
Pssm-ID: 239071 Cd Length: 339 Bit Score: 437.39 E-value: 1.06e-154
L-Aminopeptidase D-amidase/D-esterase (DmpA) family; DmpA catalyzes the release of N-terminal ...
13-341
1.06e-154
L-Aminopeptidase D-amidase/D-esterase (DmpA) family; DmpA catalyzes the release of N-terminal D and L amino acids from peptide susbtrates. DmpA is synthesized as a single polypeptide precursor, which is autocatalytically cleaved to the active heterodimeric form. The cleavage results in two polypeptide chains, with one chain containing an N-terminal nucleophile. This group represents one of the rare aminopeptidases that are not metalloenzymes. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine.
Pssm-ID: 239071 Cd Length: 339 Bit Score: 437.39 E-value: 1.06e-154
L-Aminopeptidase D-amidase/D-esterase (DmpA) family; DmpA catalyzes the release of N-terminal ...
13-341
1.06e-154
L-Aminopeptidase D-amidase/D-esterase (DmpA) family; DmpA catalyzes the release of N-terminal D and L amino acids from peptide susbtrates. DmpA is synthesized as a single polypeptide precursor, which is autocatalytically cleaved to the active heterodimeric form. The cleavage results in two polypeptide chains, with one chain containing an N-terminal nucleophile. This group represents one of the rare aminopeptidases that are not metalloenzymes. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine.
Pssm-ID: 239071 Cd Length: 339 Bit Score: 437.39 E-value: 1.06e-154
DmpA/OAT superfamily; composed of L-aminopeptidase D-amidase/D-esterase (DmpA), ornithine ...
43-317
5.32e-19
DmpA/OAT superfamily; composed of L-aminopeptidase D-amidase/D-esterase (DmpA), ornithine acetyltransferase (OAT) and similar proteins. DmpA is an aminopeptidase that releases N-terminal D and L amino acids from peptide substrates. This group represents one of the rare aminopeptidases that are not metalloenzymes. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine. OAT catalyzes the first and fifth steps in arginine biosynthesis, coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in the arginine biosynthetic pathway. The superfamily also contains an enzyme, endo-type 6-aminohexanoate-oligomer hydrolase, that have been shown to be involved in nylon degradation. Proteins in this superfamily undergo autocatalytic cleavage of an inactive precursor at the site immediately upstream to the catalytic nucleophile.
Pssm-ID: 238070 Cd Length: 286 Bit Score: 85.52 E-value: 5.32e-19
nylC-like family; composed of proteins with similarity to Flavobacterium endo-type ...
23-258
1.13e-07
nylC-like family; composed of proteins with similarity to Flavobacterium endo-type 6-aminohexanoate-oligomer hydrolase (EIII), the product of the nylon oligomer degradation gene, nylC. EIII is an amide hydrolase that catalyzes the degradation of highly-polymerized 6-aminohexanoate oligomers. Together with other nylon degradation enzymes, such as 6-aminohexanoate cyclic dimer hydrolase (EI) and 6-aminohexanoate dimer hydrolase (EII), EIII plays a role in the detoxification and biological removal of the synthetic by-products of nylon manufacture. EIII shows sequence similarity to L-aminopeptidase D-amidase/D-esterase (DmpA), an aminopeptidase that releases N-terminal D and L amino acids from peptide substrates. Like DmpA, EIII undergoes autocatalytic cleavage in front of a nucleophile to form a heterodimer. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine.
Pssm-ID: 239070 Cd Length: 260 Bit Score: 52.23 E-value: 1.13e-07
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
mapped to the query sequence.
Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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Modify your query to search against a different database and/or use advanced search options
