Dus3l protein [Mus musculus]
beta/alpha barrel domain-containing protein( domain architecture ID 229392)
beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions
List of domain hits
Name | Accession | Description | Interval | E-value | ||
TIM super family | cl21457 | TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ... |
88-162 | 4.49e-30 | ||
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure. The actual alignment was detected with superfamily member cd02801: Pssm-ID: 473867 [Multi-domain] Cd Length: 231 Bit Score: 112.59 E-value: 4.49e-30
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Name | Accession | Description | Interval | E-value | |||
DUS_like_FMN | cd02801 | Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
88-162 | 4.49e-30 | |||
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present. Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 112.59 E-value: 4.49e-30
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DusA | COG0042 | tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
88-204 | 6.90e-28 | |||
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 108.64 E-value: 6.90e-28
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Dus | pfam01207 | Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
88-157 | 2.86e-18 | |||
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria. Pssm-ID: 426126 Cd Length: 309 Bit Score: 82.76 E-value: 2.86e-18
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Name | Accession | Description | Interval | E-value | |||
DUS_like_FMN | cd02801 | Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
88-162 | 4.49e-30 | |||
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present. Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 112.59 E-value: 4.49e-30
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DusA | COG0042 | tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
88-204 | 6.90e-28 | |||
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 108.64 E-value: 6.90e-28
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Dus | pfam01207 | Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
88-157 | 2.86e-18 | |||
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria. Pssm-ID: 426126 Cd Length: 309 Bit Score: 82.76 E-value: 2.86e-18
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Blast search parameters | ||||
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