molybdenum cofactor biosynthesis protein MoaE serves as the catalytic subunit of the molybdopterin synthase complex, which catalyzes the conversion of precursor Z into molybdopterin
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; ...
3-144
6.41e-74
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; Molybdopterin synthase catalytic subunit MoaE is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440083 [Multi-domain] Cd Length: 143 Bit Score: 217.36 E-value: 6.41e-74
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
13-137
2.10e-61
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.
Pssm-ID: 238385 [Multi-domain] Cd Length: 124 Bit Score: 185.03 E-value: 2.10e-61
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of ...
8-121
2.63e-52
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of molybdopterin. Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Converting factor contains the MoaE and MoaD proteins.
Pssm-ID: 460546 Cd Length: 113 Bit Score: 161.47 E-value: 2.63e-52
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; ...
3-144
6.41e-74
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; Molybdopterin synthase catalytic subunit MoaE is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440083 [Multi-domain] Cd Length: 143 Bit Score: 217.36 E-value: 6.41e-74
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
13-137
2.10e-61
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.
Pssm-ID: 238385 [Multi-domain] Cd Length: 124 Bit Score: 185.03 E-value: 2.10e-61
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of ...
8-121
2.63e-52
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of molybdopterin. Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Converting factor contains the MoaE and MoaD proteins.
Pssm-ID: 460546 Cd Length: 113 Bit Score: 161.47 E-value: 2.63e-52
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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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,
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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,
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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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