competence/damage-inducible CinA family protein containing only the C-terminal CinA domain, similar to Pseudomonas putida nicotinamide-nucleotide (NMN) amidohydrolase PncC
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
23-164
1.81e-46
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; Nicotinamide mononucleotide (NMN) deamidase PncC is part of the Pathway/BioSystem: NAD biosynthesis
:
Pssm-ID: 441155 Cd Length: 154 Bit Score: 149.42 E-value: 1.81e-46
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
23-164
1.81e-46
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; Nicotinamide mononucleotide (NMN) deamidase PncC is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 441155 Cd Length: 154 Bit Score: 149.42 E-value: 1.81e-46
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
17-164
1.18e-41
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. This Pfam family consists of putative competence-damaged proteins from the cin operon. Some members of this family have nicotinamide mononucleotide (NMN) deamidase activity.
Pssm-ID: 460565 Cd Length: 155 Bit Score: 136.90 E-value: 1.18e-41
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ...
24-164
3.37e-31
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species. Several bacterial species have a protein consisting largely of the C-terminal domain of CinA but lacking the N-terminal domain, including nicotinamide mononucleotide (NMN) deamidase (3.5.1.42) proteins PncC in Shewanella oneidensis and ygaD in E. coli. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129303 [Multi-domain] Cd Length: 146 Bit Score: 110.19 E-value: 3.37e-31
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
23-164
1.81e-46
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; Nicotinamide mononucleotide (NMN) deamidase PncC is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 441155 Cd Length: 154 Bit Score: 149.42 E-value: 1.81e-46
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
17-164
1.18e-41
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. This Pfam family consists of putative competence-damaged proteins from the cin operon. Some members of this family have nicotinamide mononucleotide (NMN) deamidase activity.
Pssm-ID: 460565 Cd Length: 155 Bit Score: 136.90 E-value: 1.18e-41
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ...
24-164
3.37e-31
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species. Several bacterial species have a protein consisting largely of the C-terminal domain of CinA but lacking the N-terminal domain, including nicotinamide mononucleotide (NMN) deamidase (3.5.1.42) proteins PncC in Shewanella oneidensis and ygaD in E. coli. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129303 [Multi-domain] Cd Length: 146 Bit Score: 110.19 E-value: 3.37e-31
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
4-138
6.12e-23
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 161761 [Multi-domain] Cd Length: 413 Bit Score: 93.82 E-value: 6.12e-23
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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if a domain or superfamily has been annotated with functional sites (conserved features),
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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)
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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
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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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