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Conserved domains on  [gi|133778319|gb|AAH23942|]
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Dus3l protein [Mus musculus]

Protein Classification

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

Graphical summary

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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
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778319  88 LHGRSREQRYTRLADWPYIEQCaKVASPMPLFGNGDILSFEDA-NCAMQTGVAGIMVARGALLKPWLFTEIKEQRH 162
Cdd:cd02801  157 VHGRTREQRYSGPADWDYIAEI-KEAVSIPVIANGDIFSLEDAlRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
 
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
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778319  88 LHGRSREQRYTRLADWPYIEQCaKVASPMPLFGNGDILSFEDA-NCAMQTGVAGIMVARGALLKPWLFTEIKEQRH 162
Cdd:cd02801  157 VHGRTREQRYSGPADWDYIAEI-KEAVSIPVIANGDIFSLEDAlRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778319  88 LHGRSREQRYTRLADWPYIEQCAKvASPMPLFGNGDILSFEDANCAM-QTGVAGIMVARGALLKPWLFTEIKE----QRH 162
Cdd:COG0042  165 VHGRTREQRYKGPADWDAIARVKE-AVSIPVIGNGDIFSPEDAKRMLeETGCDGVMIGRGALGNPWLFREIDAylagGEA 243
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 133778319 163 WDISSSERLDILRDFTHYGLEHWGsDTQGVERTRRFLLeWLS 204
Cdd:COG0042  244 PPPSLEEVLELLLEHLELLLEFYG-ERRGLRRMRKHLL-WYF 283
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
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133778319   88 LHGRSREQRYTRLADWPYIEQcAKVASPMPLFGNGDILSFEDANCAM-QTGVAGIMVARGALLKPWLFTEI 157
Cdd:pfam01207 157 VHGRTRAQNYEGTADWDAIKQ-VKQAVSIPVIANGDITDPEDAQRCLaYTGADGVMIGRGALGNPWLFAEQ 226
 
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
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778319  88 LHGRSREQRYTRLADWPYIEQCaKVASPMPLFGNGDILSFEDA-NCAMQTGVAGIMVARGALLKPWLFTEIKEQRH 162
Cdd:cd02801  157 VHGRTREQRYSGPADWDYIAEI-KEAVSIPVIANGDIFSLEDAlRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778319  88 LHGRSREQRYTRLADWPYIEQCAKvASPMPLFGNGDILSFEDANCAM-QTGVAGIMVARGALLKPWLFTEIKE----QRH 162
Cdd:COG0042  165 VHGRTREQRYKGPADWDAIARVKE-AVSIPVIGNGDIFSPEDAKRMLeETGCDGVMIGRGALGNPWLFREIDAylagGEA 243
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 133778319 163 WDISSSERLDILRDFTHYGLEHWGsDTQGVERTRRFLLeWLS 204
Cdd:COG0042  244 PPPSLEEVLELLLEHLELLLEFYG-ERRGLRRMRKHLL-WYF 283
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
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133778319   88 LHGRSREQRYTRLADWPYIEQcAKVASPMPLFGNGDILSFEDANCAM-QTGVAGIMVARGALLKPWLFTEI 157
Cdd:pfam01207 157 VHGRTRAQNYEGTADWDAIKQ-VKQAVSIPVIANGDITDPEDAQRCLaYTGADGVMIGRGALGNPWLFAEQ 226
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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