nucleotide 5'-monophosphate nucleosidase PpnN catalyzes the hydrolysis of the N-glycosidic bond of diverse pyrimidine and purine nucleotide 5'-monophosphates, to form ribose 5-phosphate and the corresponding free base
nucleotide 5'-monophosphate nucleosidase PpnN; PpnN (pyrimidine/purine nucleotide 5'-monophosphate nucleosidase), widely conserved in gamma proteobacteria, plays a role in purine homeostasis. It can bind the the stringent response alarmones ppGpp and pppGpp and then, because of allosteric changes, have a much higher rate of cleavage of preferred substrate GMP. PpnN was previously known in E. coli as YgdH.
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Pssm-ID: 468501 [Multi-domain] Cd Length: 450 Bit Score: 900.71 E-value: 0e+00
nucleotide 5'-monophosphate nucleosidase PpnN; PpnN (pyrimidine/purine nucleotide 5'-monophosphate nucleosidase), widely conserved in gamma proteobacteria, plays a role in purine homeostasis. It can bind the the stringent response alarmones ppGpp and pppGpp and then, because of allosteric changes, have a much higher rate of cleavage of preferred substrate GMP. PpnN was previously known in E. coli as YgdH.
Pssm-ID: 468501 [Multi-domain] Cd Length: 450 Bit Score: 900.71 E-value: 0e+00
Domain of unknown function (DUF3412); This presumed domain is functionally uncharacterized. ...
333-453
8.66e-83
Domain of unknown function (DUF3412); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 120 amino acids in length. This domain is found associated with pfam03641.
Pssm-ID: 463386 Cd Length: 121 Bit Score: 250.53 E-value: 8.66e-83
TIGR00730 family protein; This model represents one branch of a subfamily of proteins of ...
151-332
2.36e-08
TIGR00730 family protein; This model represents one branch of a subfamily of proteins of unknown function. Both PSI-BLAST and weak hits by this model show a low level of similarity to and suggest an evolutionary relationship of the subfamily to the DprA/Smf family of DNA-processing proteins involved in chromosomal transformation with foreign DNA. Both Aquifex aeolicus and Mycobacterium leprae have one member in each of two branches of this subfamily, suggesting that the branches may have distinct functions. [Hypothetical proteins, Conserved]
Pssm-ID: 129813 [Multi-domain] Cd Length: 178 Bit Score: 53.67 E-value: 2.36e-08
nucleotide 5'-monophosphate nucleosidase PpnN; PpnN (pyrimidine/purine nucleotide 5'-monophosphate nucleosidase), widely conserved in gamma proteobacteria, plays a role in purine homeostasis. It can bind the the stringent response alarmones ppGpp and pppGpp and then, because of allosteric changes, have a much higher rate of cleavage of preferred substrate GMP. PpnN was previously known in E. coli as YgdH.
Pssm-ID: 468501 [Multi-domain] Cd Length: 450 Bit Score: 900.71 E-value: 0e+00
Domain of unknown function (DUF3412); This presumed domain is functionally uncharacterized. ...
333-453
8.66e-83
Domain of unknown function (DUF3412); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 120 amino acids in length. This domain is found associated with pfam03641.
Pssm-ID: 463386 Cd Length: 121 Bit Score: 250.53 E-value: 8.66e-83
Pyrimidine/purine nucleotide 5'-monophosphate nucleosidases; This is an N-terminal domain ...
3-111
7.37e-67
Pyrimidine/purine nucleotide 5'-monophosphate nucleosidases; This is an N-terminal domain found in pyrimidine/purine nucleotide 5'-monophosphate nucleosidases (PpnN) in bacteria. PpnN catalyzes the hydrolysis of the N-glycosidic bond of diverse pyrimidine and purine nucleotide 5'-monophosphates, to form ribose 5-phosphate and the corresponding free base. It can use AMP, GMP, IMP, CMP, dTMP and UMP as substrates. It is found in association with pfam03641 and pfam11892.
Pssm-ID: 434214 Cd Length: 109 Bit Score: 208.93 E-value: 7.37e-67
Possible lysine decarboxylase; The members of this family share a highly conserved motif ...
190-328
1.28e-36
Possible lysine decarboxylase; The members of this family share a highly conserved motif PGGXGTXXE that is probably functionally important. This family includes proteins annotated as lysine decarboxylases, although the evidence for this is not clear.
Pssm-ID: 397621 Cd Length: 130 Bit Score: 130.80 E-value: 1.28e-36
TIGR00730 family protein; This model represents one branch of a subfamily of proteins of ...
151-332
2.36e-08
TIGR00730 family protein; This model represents one branch of a subfamily of proteins of unknown function. Both PSI-BLAST and weak hits by this model show a low level of similarity to and suggest an evolutionary relationship of the subfamily to the DprA/Smf family of DNA-processing proteins involved in chromosomal transformation with foreign DNA. Both Aquifex aeolicus and Mycobacterium leprae have one member in each of two branches of this subfamily, suggesting that the branches may have distinct functions. [Hypothetical proteins, Conserved]
Pssm-ID: 129813 [Multi-domain] Cd Length: 178 Bit Score: 53.67 E-value: 2.36e-08
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.
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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.
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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
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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
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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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