electron transfer flavoprotein (ETF) subunit beta/FixA family protein similar to the beta subunit of ETF, which transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase, and protein FixA, which plays a role in a redox process involved in nitrogen fixation
electron transfer flavoprotein (ETF) beta; The electron transfer flavoprotein (ETF) serves as ...
5-215
1.48e-90
electron transfer flavoprotein (ETF) beta; The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is a heterodimer, consisting of an alpha and a beta subunit, which binds one molecule of FAD per dimer. A similar system also exists in some bacteria. The homologous pair of proteins (FixA/FixB) are essential for nitrogen fixation. The beta subunit is distantly related to and forms a heterodimer with the alpha subunit.
Pssm-ID: 467487 Cd Length: 210 Bit Score: 266.32 E-value: 1.48e-90
Electron transfer flavoprotein domain; Electron transfer flavoproteins (ETFs) serve as ...
34-212
5.13e-43
Electron transfer flavoprotein domain; Electron transfer flavoproteins (ETFs) serve as specific electron acceptors for primary dehydrogenases, transferring the electrons to terminal respiratory systems. They can be functionally classified into constitutive, "housekeeping" ETFs, mainly involved in the oxidation of fatty acids (Group I), and ETFs produced by some prokaryotes under specific growth conditions, receiving electrons only from the oxidation of specific substrates (Group II). ETFs are heterodimeric proteins composed of an alpha and beta subunit, and contain an FAD cofactor and AMP. ETF consists of three domains: domains I and II are formed by the N- and C-terminal portions of the alpha subunit, respectively, while domain III is formed by the beta subunit. Domains I and III share an almost identical alpha-beta-alpha sandwich fold, while domain II forms an alpha-beta-alpha sandwich similar to that of bacterial flavodoxins. FAD is bound in a cleft between domains II and III, while domain III binds the AMP molecule. Interactions between domains I and III stabilise the protein, forming a shallow bowl where domain II resides. This entry represents the N-terminal domain of both the alpha and beta subunits from Group I and Group II ETFs.
Pssm-ID: 214890 [Multi-domain] Cd Length: 185 Bit Score: 144.33 E-value: 5.13e-43
Electron transfer flavoprotein domain; This family includes the homologous domain shared ...
38-214
4.26e-34
Electron transfer flavoprotein domain; This family includes the homologous domain shared between the alpha and beta subunits of the electron transfer flavoprotein.
Pssm-ID: 425985 [Multi-domain] Cd Length: 178 Bit Score: 121.18 E-value: 4.26e-34
electron transfer flavoprotein (ETF) beta; The electron transfer flavoprotein (ETF) serves as ...
5-215
1.48e-90
electron transfer flavoprotein (ETF) beta; The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is a heterodimer, consisting of an alpha and a beta subunit, which binds one molecule of FAD per dimer. A similar system also exists in some bacteria. The homologous pair of proteins (FixA/FixB) are essential for nitrogen fixation. The beta subunit is distantly related to and forms a heterodimer with the alpha subunit.
Pssm-ID: 467487 Cd Length: 210 Bit Score: 266.32 E-value: 1.48e-90
Electron transfer flavoprotein domain; Electron transfer flavoproteins (ETFs) serve as ...
34-212
5.13e-43
Electron transfer flavoprotein domain; Electron transfer flavoproteins (ETFs) serve as specific electron acceptors for primary dehydrogenases, transferring the electrons to terminal respiratory systems. They can be functionally classified into constitutive, "housekeeping" ETFs, mainly involved in the oxidation of fatty acids (Group I), and ETFs produced by some prokaryotes under specific growth conditions, receiving electrons only from the oxidation of specific substrates (Group II). ETFs are heterodimeric proteins composed of an alpha and beta subunit, and contain an FAD cofactor and AMP. ETF consists of three domains: domains I and II are formed by the N- and C-terminal portions of the alpha subunit, respectively, while domain III is formed by the beta subunit. Domains I and III share an almost identical alpha-beta-alpha sandwich fold, while domain II forms an alpha-beta-alpha sandwich similar to that of bacterial flavodoxins. FAD is bound in a cleft between domains II and III, while domain III binds the AMP molecule. Interactions between domains I and III stabilise the protein, forming a shallow bowl where domain II resides. This entry represents the N-terminal domain of both the alpha and beta subunits from Group I and Group II ETFs.
Pssm-ID: 214890 [Multi-domain] Cd Length: 185 Bit Score: 144.33 E-value: 5.13e-43
Electron transfer flavoprotein domain; This family includes the homologous domain shared ...
38-214
4.26e-34
Electron transfer flavoprotein domain; This family includes the homologous domain shared between the alpha and beta subunits of the electron transfer flavoprotein.
Pssm-ID: 425985 [Multi-domain] Cd Length: 178 Bit Score: 121.18 E-value: 4.26e-34
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.
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
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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
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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