Methyl-coenzyme M reductase (MCR) gamma subunit. MCR catalyzes the terminal step of methane ...
5-256
1.60e-96
Methyl-coenzyme M reductase (MCR) gamma subunit. MCR catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea, in which methyl-coenzyme M and coenzyme B are converted to methane and the heterodisulfide of coenzyme M and coenzyme B (CoM-S-S-CoB). MCR is a dimer of trimers, each of which consists of one alpha, one beta, and one gamma subunit, with two identical active sites containing nickel porphinoid factor 430 (F430).
The actual alignment was detected with superfamily member pfam02240:
Pssm-ID: 469684 Cd Length: 246 Bit Score: 283.09 E-value: 1.60e-96
Methyl-coenzyme M reductase gamma subunit; Methyl-coenzyme M reductase (MCR) is the enzyme ...
5-256
1.60e-96
Methyl-coenzyme M reductase gamma subunit; Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (pfam02249), 2 beta (pfam02241), and 2 gamma (this family) subunits with two identical nickel porphinoid active sites.
Pssm-ID: 396698 Cd Length: 246 Bit Score: 283.09 E-value: 1.60e-96
Methyl-coenzyme M reductase (MCR) gamma subunit. MCR catalyzes the terminal step of methane ...
6-260
1.90e-88
Methyl-coenzyme M reductase (MCR) gamma subunit. MCR catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea, in which methyl-coenzyme M and coenzyme B are converted to methane and the heterodisulfide of coenzyme M and coenzyme B (CoM-S-S-CoB). MCR is a dimer of trimers, each of which consists of one alpha, one beta, and one gamma subunit, with two identical active sites containing nickel porphinoid factor 430 (F430).
Pssm-ID: 238301 Cd Length: 246 Bit Score: 262.81 E-value: 1.90e-88
methyl-coenzyme M reductase, gamma subunit; Members of this protein family are the gamma ...
6-256
3.49e-77
methyl-coenzyme M reductase, gamma subunit; Members of this protein family are the gamma subunit of methyl coenzyme M reductase, also called coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1). This enzyme, with alpha, beta, and gamma subunits, catalyzes the last step in methanogenesis. Several methanogens have encode two such enzymes, designated I and II; this model does not separate the isozymes. [Energy metabolism, Methanogenesis]
Pssm-ID: 132303 Cd Length: 244 Bit Score: 234.00 E-value: 3.49e-77
Methyl-coenzyme M reductase gamma subunit; Methyl-coenzyme M reductase (MCR) is the enzyme ...
5-256
1.60e-96
Methyl-coenzyme M reductase gamma subunit; Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (pfam02249), 2 beta (pfam02241), and 2 gamma (this family) subunits with two identical nickel porphinoid active sites.
Pssm-ID: 396698 Cd Length: 246 Bit Score: 283.09 E-value: 1.60e-96
Methyl-coenzyme M reductase (MCR) gamma subunit. MCR catalyzes the terminal step of methane ...
6-260
1.90e-88
Methyl-coenzyme M reductase (MCR) gamma subunit. MCR catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea, in which methyl-coenzyme M and coenzyme B are converted to methane and the heterodisulfide of coenzyme M and coenzyme B (CoM-S-S-CoB). MCR is a dimer of trimers, each of which consists of one alpha, one beta, and one gamma subunit, with two identical active sites containing nickel porphinoid factor 430 (F430).
Pssm-ID: 238301 Cd Length: 246 Bit Score: 262.81 E-value: 1.90e-88
methyl-coenzyme M reductase, gamma subunit; Members of this protein family are the gamma ...
6-256
3.49e-77
methyl-coenzyme M reductase, gamma subunit; Members of this protein family are the gamma subunit of methyl coenzyme M reductase, also called coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1). This enzyme, with alpha, beta, and gamma subunits, catalyzes the last step in methanogenesis. Several methanogens have encode two such enzymes, designated I and II; this model does not separate the isozymes. [Energy metabolism, Methanogenesis]
Pssm-ID: 132303 Cd Length: 244 Bit Score: 234.00 E-value: 3.49e-77
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)
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
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