formate dehydrogenase accessory protein FdhE; This model describes an accessory protein ...
2-306
3.56e-167
formate dehydrogenase accessory protein FdhE; This model describes an accessory protein required for the assembly of formate dehydrogenase of certain proteobacteria although not present in the final complex. The exact nature of the function of FdhE in the assembly of the complex is unknown, but considering the presence of selenocysteine, molybdopterin, iron-sulfur clusters and cytochrome b556, it is likely to have something to do with the insertion of cofactors. The only sequence scoring between trusted and noise is that from Aquifex aeolicus, which shows certain structural differences from the proteobacterial forms in the alignment. However it is notable that A. aeolicus also has a sequence scoring above trusted to the alpha subunit of formate dehydrogenase (TIGR01553).
:
Pssm-ID: 130625 Cd Length: 305 Bit Score: 466.33 E-value: 3.56e-167
formate dehydrogenase accessory protein FdhE; This model describes an accessory protein ...
2-306
3.56e-167
formate dehydrogenase accessory protein FdhE; This model describes an accessory protein required for the assembly of formate dehydrogenase of certain proteobacteria although not present in the final complex. The exact nature of the function of FdhE in the assembly of the complex is unknown, but considering the presence of selenocysteine, molybdopterin, iron-sulfur clusters and cytochrome b556, it is likely to have something to do with the insertion of cofactors. The only sequence scoring between trusted and noise is that from Aquifex aeolicus, which shows certain structural differences from the proteobacterial forms in the alignment. However it is notable that A. aeolicus also has a sequence scoring above trusted to the alpha subunit of formate dehydrogenase (TIGR01553).
Pssm-ID: 130625 Cd Length: 305 Bit Score: 466.33 E-value: 3.56e-167
Protein involved in formate dehydrogenase formation; The function of these proteins is unknown. ...
15-304
2.80e-129
Protein involved in formate dehydrogenase formation; The function of these proteins is unknown. They may possibly be involved in the formation of formate dehydrogenase.
Pssm-ID: 427792 Cd Length: 286 Bit Score: 369.65 E-value: 2.80e-129
formate dehydrogenase accessory protein FdhE and similar proteins; This family contains ...
46-294
1.95e-63
formate dehydrogenase accessory protein FdhE and similar proteins; This family contains formate dehydrogenase accessory protein FdhE and FdhE-like protein, found largely in gamma- and some beta-Proteobacteria, where the fdhE genes are almost always genetically-linked to the structural genes for formate dehydrogenases. FdhE is required for the assembly of formate dehydrogenase although not present in the final complex. In E. coli, FdhE interacts with the catalytic subunits of the respiratory formate dehydrogenases. Purification of recombinant FdhE demonstrates the protein is an iron-binding rubredoxin that can adopt monomeric and homodimeric forms. E. coli FdhE interacts with the catalytic subunits, FdnG and FdoG, of the Tat- dependent respiratory formate dehydrogenases. Site-directed mutagenesis has shown that conserved cysteine motifs are essential for the physiological activity of the FdhE protein and are also involved in Fe(III) ligation. The iron likely is redox active, suggesting that the switch from aerobic to anaerobic conditions may be important in modulating FdhE function. Alternatively, FdhE may be involved in an electron transfer reaction, similar to other rubredoxins.
Pssm-ID: 319975 Cd Length: 257 Bit Score: 201.06 E-value: 1.95e-63
formate dehydrogenase accessory protein FdhE; This model describes an accessory protein ...
2-306
3.56e-167
formate dehydrogenase accessory protein FdhE; This model describes an accessory protein required for the assembly of formate dehydrogenase of certain proteobacteria although not present in the final complex. The exact nature of the function of FdhE in the assembly of the complex is unknown, but considering the presence of selenocysteine, molybdopterin, iron-sulfur clusters and cytochrome b556, it is likely to have something to do with the insertion of cofactors. The only sequence scoring between trusted and noise is that from Aquifex aeolicus, which shows certain structural differences from the proteobacterial forms in the alignment. However it is notable that A. aeolicus also has a sequence scoring above trusted to the alpha subunit of formate dehydrogenase (TIGR01553).
Pssm-ID: 130625 Cd Length: 305 Bit Score: 466.33 E-value: 3.56e-167
Protein involved in formate dehydrogenase formation; The function of these proteins is unknown. ...
15-304
2.80e-129
Protein involved in formate dehydrogenase formation; The function of these proteins is unknown. They may possibly be involved in the formation of formate dehydrogenase.
Pssm-ID: 427792 Cd Length: 286 Bit Score: 369.65 E-value: 2.80e-129
formate dehydrogenase accessory protein FdhE and similar proteins; This family contains ...
46-294
1.95e-63
formate dehydrogenase accessory protein FdhE and similar proteins; This family contains formate dehydrogenase accessory protein FdhE and FdhE-like protein, found largely in gamma- and some beta-Proteobacteria, where the fdhE genes are almost always genetically-linked to the structural genes for formate dehydrogenases. FdhE is required for the assembly of formate dehydrogenase although not present in the final complex. In E. coli, FdhE interacts with the catalytic subunits of the respiratory formate dehydrogenases. Purification of recombinant FdhE demonstrates the protein is an iron-binding rubredoxin that can adopt monomeric and homodimeric forms. E. coli FdhE interacts with the catalytic subunits, FdnG and FdoG, of the Tat- dependent respiratory formate dehydrogenases. Site-directed mutagenesis has shown that conserved cysteine motifs are essential for the physiological activity of the FdhE protein and are also involved in Fe(III) ligation. The iron likely is redox active, suggesting that the switch from aerobic to anaerobic conditions may be important in modulating FdhE function. Alternatively, FdhE may be involved in an electron transfer reaction, similar to other rubredoxins.
Pssm-ID: 319975 Cd Length: 257 Bit Score: 201.06 E-value: 1.95e-63
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
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
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
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
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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
(CDART).
Modify your query to search against a different database and/or use advanced search options
