polyphenol oxidase/laccase family protein such as peptidoglycan editing factor PgeF involved in the maintenance of bacterial peptide composition; may bind copper and oxidize one or more of a variety of phenolic and non-phenolic compounds
Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able ...
20-239
1.55e-97
Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able to oxidize a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms.
Pssm-ID: 460601 [Multi-domain] Cd Length: 232 Bit Score: 284.38 E-value: 1.55e-97
YfiH family protein; PSI-BLAST converges on members of this family of uncharacterized ...
25-240
9.88e-74
YfiH family protein; PSI-BLAST converges on members of this family of uncharacterized bacterial proteins and shows no significant similarity to any characterized protein. No completed genome to date has two members. Members of the family have been crystallized but the function is unknown. [Unknown function, General]
Pssm-ID: 273235 [Multi-domain] Cd Length: 221 Bit Score: 223.42 E-value: 9.88e-74
protein of unknown function YfiH; This subfamily contains YfiH, a protein of unknown function ...
61-239
1.25e-66
protein of unknown function YfiH; This subfamily contains YfiH, a protein of unknown function from Shigella flexneri, E. coli, and many similar proteins which collectively are often called DUF152. The structure of YfiH reveals a distant homology to Rho-activating toxins cytotoxic necrotizing factor 1 (CNF1) as well as chemotaxis protein CheD that stimulates methylation of methyl-accepting chemotaxis proteins (MCPs), all having an invariant Cys-His pair forming a catalytic dyad, and is required by the CNF-1 toxins for deamidation activity.
Pssm-ID: 319354 Cd Length: 185 Bit Score: 203.97 E-value: 1.25e-66
Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able ...
20-239
1.55e-97
Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able to oxidize a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms.
Pssm-ID: 460601 [Multi-domain] Cd Length: 232 Bit Score: 284.38 E-value: 1.55e-97
YfiH family protein; PSI-BLAST converges on members of this family of uncharacterized ...
25-240
9.88e-74
YfiH family protein; PSI-BLAST converges on members of this family of uncharacterized bacterial proteins and shows no significant similarity to any characterized protein. No completed genome to date has two members. Members of the family have been crystallized but the function is unknown. [Unknown function, General]
Pssm-ID: 273235 [Multi-domain] Cd Length: 221 Bit Score: 223.42 E-value: 9.88e-74
protein of unknown function YfiH; This subfamily contains YfiH, a protein of unknown function ...
61-239
1.25e-66
protein of unknown function YfiH; This subfamily contains YfiH, a protein of unknown function from Shigella flexneri, E. coli, and many similar proteins which collectively are often called DUF152. The structure of YfiH reveals a distant homology to Rho-activating toxins cytotoxic necrotizing factor 1 (CNF1) as well as chemotaxis protein CheD that stimulates methylation of methyl-accepting chemotaxis proteins (MCPs), all having an invariant Cys-His pair forming a catalytic dyad, and is required by the CNF-1 toxins for deamidation activity.
Pssm-ID: 319354 Cd Length: 185 Bit Score: 203.97 E-value: 1.25e-66
cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and YfiH (DUF152) are distant ...
84-172
1.23e-03
cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and YfiH (DUF152) are distant homologs; This family contains distant homologs that include cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and a protein of unknown function YfiH. CNF-1 along with dermonecrotic toxin (DNT) from Bordetella species, and Burkholderia Lethal Factor 1 (BLF1, also known as BPSL1549) are Rho-activating toxins. The bacterial chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins (MCPs). YfiH, a domain of unknown function, also included in this family reveals a structure with a distant homology between to the CNF1, and CheD, all having an invariant Cys-His pair forming a catalytic dyad that is required by the CNF-1 toxins for deamidation activity.
Pssm-ID: 319353 Cd Length: 145 Bit Score: 38.15 E-value: 1.23e-03
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),
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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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