8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
11-322
0e+00
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]
:
Pssm-ID: 211589 [Multi-domain] Cd Length: 310 Bit Score: 526.79 E-value: 0e+00
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
11-322
0e+00
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 211589 [Multi-domain] Cd Length: 310 Bit Score: 526.79 E-value: 0e+00
8-oxoguanine DNA glycosylase, N-terminal domain; The presence of 8-oxoguanine residues in DNA ...
25-141
1.07e-42
8-oxoguanine DNA glycosylase, N-terminal domain; The presence of 8-oxoguanine residues in DNA can give rise to G-C to T-A transversion mutations. This enzyme is found in archaeal, bacterial and eukaryotic species, and is specifically responsible for the process which leads to the removal of 8-oxoguanine residues. It has DNA glycosylase activity (EC:3.2.2.23) and DNA lyase activity (EC:4.2.99.18). The region featured in this family is the N-terminal domain, which is organized into a single copy of a TBP-like fold. The domain contributes residues to the 8-oxoguanine binding pocket.
Pssm-ID: 429744 Cd Length: 115 Bit Score: 145.84 E-value: 1.07e-42
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
139-319
2.85e-35
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 238013 [Multi-domain] Cd Length: 158 Bit Score: 127.74 E-value: 2.85e-35
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
11-322
0e+00
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 211589 [Multi-domain] Cd Length: 310 Bit Score: 526.79 E-value: 0e+00
8-oxoguanine DNA glycosylase, N-terminal domain; The presence of 8-oxoguanine residues in DNA ...
25-141
1.07e-42
8-oxoguanine DNA glycosylase, N-terminal domain; The presence of 8-oxoguanine residues in DNA can give rise to G-C to T-A transversion mutations. This enzyme is found in archaeal, bacterial and eukaryotic species, and is specifically responsible for the process which leads to the removal of 8-oxoguanine residues. It has DNA glycosylase activity (EC:3.2.2.23) and DNA lyase activity (EC:4.2.99.18). The region featured in this family is the N-terminal domain, which is organized into a single copy of a TBP-like fold. The domain contributes residues to the 8-oxoguanine binding pocket.
Pssm-ID: 429744 Cd Length: 115 Bit Score: 145.84 E-value: 1.07e-42
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
139-319
2.85e-35
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 238013 [Multi-domain] Cd Length: 158 Bit Score: 127.74 E-value: 2.85e-35
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
143-309
1.06e-23
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.
Pssm-ID: 425841 [Multi-domain] Cd Length: 141 Bit Score: 95.81 E-value: 1.06e-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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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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