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tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X3 [Mus musculus]
tRNA-dihydrouridine synthase family protein( domain architecture ID 14390137)
tRNA-dihydrouridine synthase family protein such as tRNA-dihydrouridine synthase, which catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs
List of domain hits
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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 ... |
1-139 | 2.96e-55 | |||
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: 181.15 E-value: 2.96e-55
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DSRM_DUS2L | cd19871 | double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) ... |
256-323 | 6.07e-38 | |||
double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins; DUS2L (also known as dihydrouridine synthase 2 (DUS2), up-regulated in lung cancer protein 8 (URLC8), or tRNA-dihydrouridine synthase 2-like) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. It negatively regulates the activation of EIF2AK2/PKR. DUS2L contains an N-terminal FMN-binding domain and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure. : Pssm-ID: 380700 Cd Length: 68 Bit Score: 130.86 E-value: 6.07e-38
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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 ... |
1-139 | 2.96e-55 | ||||
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: 181.15 E-value: 2.96e-55
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DSRM_DUS2L | cd19871 | double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) ... |
256-323 | 6.07e-38 | ||||
double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins; DUS2L (also known as dihydrouridine synthase 2 (DUS2), up-regulated in lung cancer protein 8 (URLC8), or tRNA-dihydrouridine synthase 2-like) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. It negatively regulates the activation of EIF2AK2/PKR. DUS2L contains an N-terminal FMN-binding domain and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure. Pssm-ID: 380700 Cd Length: 68 Bit Score: 130.86 E-value: 6.07e-38
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DusA | COG0042 | tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
1-165 | 2.64e-36 | ||||
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: 134.07 E-value: 2.64e-36
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Dus | pfam01207 | Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
1-211 | 4.47e-35 | ||||
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: 130.91 E-value: 4.47e-35
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nifR3_yhdG | TIGR00737 | putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
1-139 | 2.13e-30 | ||||
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General] Pssm-ID: 129820 Cd Length: 319 Bit Score: 118.62 E-value: 2.13e-30
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PRK10415 | PRK10415 | tRNA-dihydrouridine synthase B; Provisional |
1-139 | 7.08e-21 | ||||
tRNA-dihydrouridine synthase B; Provisional Pssm-ID: 182440 Cd Length: 321 Bit Score: 91.96 E-value: 7.08e-21
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DSRM | smart00358 | Double-stranded RNA binding motif; |
257-320 | 2.05e-08 | ||||
Double-stranded RNA binding motif; Pssm-ID: 214634 [Multi-domain] Cd Length: 67 Bit Score: 50.34 E-value: 2.05e-08
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dsrm | pfam00035 | Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ... |
257-319 | 1.03e-07 | ||||
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA. Pssm-ID: 425434 [Multi-domain] Cd Length: 66 Bit Score: 48.38 E-value: 1.03e-07
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Rnc | COG0571 | dsRNA-specific ribonuclease [Transcription]; |
257-314 | 2.16e-05 | ||||
dsRNA-specific ribonuclease [Transcription]; Pssm-ID: 440336 [Multi-domain] Cd Length: 229 Bit Score: 45.09 E-value: 2.16e-05
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RNaseIII | TIGR02191 | ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. ... |
257-318 | 9.74e-05 | ||||
ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. This enzyme cleaves double-stranded rRNA. It is involved in processing ribosomal RNA precursors. It is found even in minimal genones such as Mycoplasma genitalium and Buchnera aphidicola, and in some cases has been shown to be an essential gene. These bacterial proteins contain a double-stranded RNA binding motif (pfam00035) and a ribonuclease III domain (pfam00636). Eukaryotic homologs tend to be much longer proteins with additional domains, localized to the nucleus, and not included in this family. [Transcription, RNA processing] Pssm-ID: 274024 [Multi-domain] Cd Length: 220 Bit Score: 43.35 E-value: 9.74e-05
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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 ... |
1-139 | 2.96e-55 | ||||
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: 181.15 E-value: 2.96e-55
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DSRM_DUS2L | cd19871 | double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) ... |
256-323 | 6.07e-38 | ||||
double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins; DUS2L (also known as dihydrouridine synthase 2 (DUS2), up-regulated in lung cancer protein 8 (URLC8), or tRNA-dihydrouridine synthase 2-like) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. It negatively regulates the activation of EIF2AK2/PKR. DUS2L contains an N-terminal FMN-binding domain and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure. Pssm-ID: 380700 Cd Length: 68 Bit Score: 130.86 E-value: 6.07e-38
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DusA | COG0042 | tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
1-165 | 2.64e-36 | ||||
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: 134.07 E-value: 2.64e-36
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Dus | pfam01207 | Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
1-211 | 4.47e-35 | ||||
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: 130.91 E-value: 4.47e-35
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nifR3_yhdG | TIGR00737 | putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
1-139 | 2.13e-30 | ||||
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General] Pssm-ID: 129820 Cd Length: 319 Bit Score: 118.62 E-value: 2.13e-30
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PRK10415 | PRK10415 | tRNA-dihydrouridine synthase B; Provisional |
1-139 | 7.08e-21 | ||||
tRNA-dihydrouridine synthase B; Provisional Pssm-ID: 182440 Cd Length: 321 Bit Score: 91.96 E-value: 7.08e-21
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PRK10550 | PRK10550 | tRNA dihydrouridine(16) synthase DusC; |
2-162 | 2.60e-13 | ||||
tRNA dihydrouridine(16) synthase DusC; Pssm-ID: 236713 Cd Length: 312 Bit Score: 69.84 E-value: 2.60e-13
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PRK11815 | PRK11815 | tRNA dihydrouridine(20/20a) synthase DusA; |
2-161 | 3.81e-10 | ||||
tRNA dihydrouridine(20/20a) synthase DusA; Pssm-ID: 236991 [Multi-domain] Cd Length: 333 Bit Score: 60.53 E-value: 3.81e-10
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DSRM_SF | cd00048 | double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ... |
263-318 | 1.56e-09 | ||||
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 amino acid domain that adopts an alpha-beta-beta-beta-alpha fold. It is not sequence specific, but highly specific for double-stranded RNAs (dsRNAs) of various origin and structure. The DSRM domains are found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila Staufen protein, E. coli RNase III, RNase H1, and dsRNA dependent adenosine deaminases. They are involved in numerous cellular mechanisms ranging from localization and transport of messenger RNAs, through maturation and degradation of RNAs, to viral response and signal transduction. Some members harbor tandem DSRMs that act in small RNA biogenesis. Pssm-ID: 380679 [Multi-domain] Cd Length: 57 Bit Score: 53.44 E-value: 1.56e-09
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DSRM_SON-like | cd19870 | double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ... |
257-323 | 5.42e-09 | ||||
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known as Bax antagonist selected in saccharomyces 1 (BASS1), negative regulatory element-binding protein (NRE-binding protein), or protein DBP-5, or SON3) is an RNA-binding protein which acts as an mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. It specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Members of this group contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. Pssm-ID: 380699 Cd Length: 75 Bit Score: 52.28 E-value: 5.42e-09
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DSRM_RNAse_III_family | cd10845 | double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ... |
257-319 | 5.91e-09 | ||||
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase III (EC 3.1.26.3; also known as ribonuclease 3) digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. It is involved in the processing of rRNA precursors, viral transcripts, some mRNAs, and at least 1 tRNA (metY, a minor form of tRNA-init-Met). It cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs. The cleavage can occur in assembled 30S, 50S, and even 70S subunits and is influenced by the presence of ribosomal proteins. The RNase III family also includes the mitochondrion-specific ribosomal protein mL44 subfamily, which is composed of mitochondrial 54S ribosomal protein L3 (MRPL3) and mitochondrial 39S ribosomal protein L44 (MRPL44). Members of this family contain an RNase III domain and a C-terminal double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. Pssm-ID: 380682 [Multi-domain] Cd Length: 69 Bit Score: 52.11 E-value: 5.91e-09
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DSRM | smart00358 | Double-stranded RNA binding motif; |
257-320 | 2.05e-08 | ||||
Double-stranded RNA binding motif; Pssm-ID: 214634 [Multi-domain] Cd Length: 67 Bit Score: 50.34 E-value: 2.05e-08
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DSRM_AtDRB-like | cd19878 | double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins ... |
258-322 | 3.28e-08 | ||||
double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRBs)and similar proteins; This family includes a group of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRB1-5). They bind double-stranded RNA (dsRNA) and may be involved in RNA-mediated silencing. Members of this family contain two to three double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. Pssm-ID: 380707 [Multi-domain] Cd Length: 67 Bit Score: 49.82 E-value: 3.28e-08
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dsrm | pfam00035 | Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ... |
257-319 | 1.03e-07 | ||||
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA. Pssm-ID: 425434 [Multi-domain] Cd Length: 66 Bit Score: 48.38 E-value: 1.03e-07
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DHOD_DHPD_FMN | cd02810 | Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
2-141 | 7.15e-07 | ||||
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue. Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 50.43 E-value: 7.15e-07
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Rnc | COG0571 | dsRNA-specific ribonuclease [Transcription]; |
257-314 | 2.16e-05 | ||||
dsRNA-specific ribonuclease [Transcription]; Pssm-ID: 440336 [Multi-domain] Cd Length: 229 Bit Score: 45.09 E-value: 2.16e-05
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OYE_like_FMN_family | cd02803 | Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
48-136 | 5.96e-05 | ||||
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 44.49 E-value: 5.96e-05
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DSRM_DGCR8_rpt1 | cd19867 | first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ... |
256-314 | 7.18e-05 | ||||
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and similar proteins; DGCR8 is a component of the microprocessor complex that acts as an RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Within the microprocessor complex, DGCR8 functions as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11bp away from the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. DGCR8 contains two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. Pssm-ID: 380696 Cd Length: 74 Bit Score: 40.78 E-value: 7.18e-05
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RNaseIII | TIGR02191 | ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. ... |
257-318 | 9.74e-05 | ||||
ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. This enzyme cleaves double-stranded rRNA. It is involved in processing ribosomal RNA precursors. It is found even in minimal genones such as Mycoplasma genitalium and Buchnera aphidicola, and in some cases has been shown to be an essential gene. These bacterial proteins contain a double-stranded RNA binding motif (pfam00035) and a ribonuclease III domain (pfam00636). Eukaryotic homologs tend to be much longer proteins with additional domains, localized to the nucleus, and not included in this family. [Transcription, RNA processing] Pssm-ID: 274024 [Multi-domain] Cd Length: 220 Bit Score: 43.35 E-value: 9.74e-05
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DSRM_AtDRB-like_rpt1 | cd19907 | first double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding ... |
261-320 | 1.48e-04 | ||||
first double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRBs)and similar proteins; This family includes a group of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRB1-5). They bind double-stranded RNA (dsRNA) and may be involved in RNA-mediated silencing. Members of this family contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. Pssm-ID: 380736 [Multi-domain] Cd Length: 69 Bit Score: 39.77 E-value: 1.48e-04
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DHOD_1B_like | cd04740 | Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
3-154 | 2.25e-04 | ||||
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 42.54 E-value: 2.25e-04
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FadH | COG1902 | 2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
48-136 | 3.95e-04 | ||||
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion]; Pssm-ID: 441506 [Multi-domain] Cd Length: 365 Bit Score: 42.08 E-value: 3.95e-04
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DHPD_FMN | cd02940 | Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
2-133 | 2.50e-03 | ||||
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue. Pssm-ID: 239244 Cd Length: 299 Bit Score: 39.19 E-value: 2.50e-03
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HisF | COG0107 | Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
84-139 | 5.54e-03 | ||||
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 439877 Cd Length: 251 Bit Score: 38.08 E-value: 5.54e-03
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Blast search parameters | ||||
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