OsmC (osmotically inducible protein C) family protein may function as a peroxiredoxin or hydroperoxide reductase, catalyzing the reduction of organic and inorganic peroxide substrates to protect the cell against oxidative stress
OsmC-like protein; Osmotically inducible protein C (OsmC) is a stress -induced protein found ...
39-141
2.67e-17
OsmC-like protein; Osmotically inducible protein C (OsmC) is a stress -induced protein found in E. Coli. This family also contains a organic hydroperoxide detoxification protein that has a novel pattern of oxidative stress regulation.
Pssm-ID: 460594 Cd Length: 99 Bit Score: 71.97 E-value: 2.67e-17
OsmC-like protein; Osmotically inducible protein C (OsmC) is a stress -induced protein found ...
39-141
2.67e-17
OsmC-like protein; Osmotically inducible protein C (OsmC) is a stress -induced protein found in E. Coli. This family also contains a organic hydroperoxide detoxification protein that has a novel pattern of oxidative stress regulation.
Pssm-ID: 460594 Cd Length: 99 Bit Score: 71.97 E-value: 2.67e-17
peroxiredoxin, Ohr subfamily; pfam02566, OsmC-like protein, contains several deeply split clades of homologous proteins. The clade modeled here includes the protein Ohr, or organic hydroperoxide resistance protein. [Cellular processes, Detoxification]
Pssm-ID: 274649 Cd Length: 134 Bit Score: 54.49 E-value: 3.41e-10
peroxiredoxin, OsmC subfamily; pfam02566, OsmC-like protein, contains several deeply split clades of homologous proteins. The clade modeled here includes the protein OsmC, or osmotically induced protein C. The member from Thermus thermophilus was shown to have hydroperoxide peroxidase activity. In many species, this protein is induced by stress and helps resist oxidative stress. [Cellular processes, Detoxification]
Pssm-ID: 274650 Cd Length: 135 Bit Score: 39.88 E-value: 8.59e-05
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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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.
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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.
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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.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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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
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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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