molybdenum cofactor biosynthesis protein B (MoaB) similar to Pyrococcus furiosus MoaB; may be a metal-binding pterin (MPT)-adenylyltransferase which converts MPT to adenylylated MPT (MPT-AMP)
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
22-187
2.23e-42
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
:
Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 139.87 E-value: 2.23e-42
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
22-187
2.23e-42
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 139.87 E-value: 2.23e-42
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
30-183
4.56e-38
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.
Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 128.36 E-value: 4.56e-38
molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB ...
27-176
6.43e-38
molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB protein molybdopterin biosynthesis regions in Proteobacteria. This crystallized but incompletely characterized protein is thought to be involved in, though not required for, early steps in molybdopterin biosynthesis. It may bind a molybdopterin precursor. A distinctive conserved motif PCN near the C-terminus helps distinguish this clade from other homologs, including sets of proteins designated MogA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
Pssm-ID: 131715 [Multi-domain] Cd Length: 163 Bit Score: 128.31 E-value: 6.43e-38
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
31-172
8.01e-15
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 68.00 E-value: 8.01e-15
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
31-179
2.46e-13
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 64.19 E-value: 2.46e-13
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
22-187
2.23e-42
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 139.87 E-value: 2.23e-42
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
30-183
4.56e-38
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.
Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 128.36 E-value: 4.56e-38
molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB ...
27-176
6.43e-38
molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB protein molybdopterin biosynthesis regions in Proteobacteria. This crystallized but incompletely characterized protein is thought to be involved in, though not required for, early steps in molybdopterin biosynthesis. It may bind a molybdopterin precursor. A distinctive conserved motif PCN near the C-terminus helps distinguish this clade from other homologs, including sets of proteins designated MogA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
Pssm-ID: 131715 [Multi-domain] Cd Length: 163 Bit Score: 128.31 E-value: 6.43e-38
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
30-168
2.76e-17
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 74.66 E-value: 2.76e-17
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
31-172
8.01e-15
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 68.00 E-value: 8.01e-15
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
30-173
1.32e-13
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin.
Pssm-ID: 238387 [Multi-domain] Cd Length: 133 Bit Score: 64.67 E-value: 1.32e-13
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
31-179
2.46e-13
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 64.19 E-value: 2.46e-13
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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