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Conserved domains on  [gi|578832039|ref|XP_006722352|]
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tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like isoform X6 [Homo sapiens]

Protein Classification

tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like( domain architecture ID 12928636)

tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like (DUS1L) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs

CATH:  3.20.20.70
EC:  1.3.1.88
Gene Symbol:  DUS1L
Gene Ontology:  GO:0050660|GO:0017150|GO:0002943
SCOP:  4000080

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
18-233 3.78e-91

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: 275.91  E-value: 3.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  18 RHVVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVRDANYRKENLYCevCPEDRPLIVQFCANDPEVFVQAALLAQD 97
Cdd:cd02801    1 KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTR--NPEERPLIVQLGGSDPETLAEAAKIVEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  98 -YCDAIDLNLGCPQMIAKR-----VLLAH------------EKLSVPVTCKIRVFPEID-KTVRYAQMLEKAGCQLLTVH 158
Cdd:cd02801   79 lGADGIDLNMGCPSPKVTKggagaALLKDpelvaeivravrEAVPIPVTVKIRLGWDDEeETLELAKALEDAGASALTVH 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578832039 159 GRTKEQKgpLSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPALFEGRSPAVW 233
Cdd:cd02801  159 GRTREQR--YSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
put_zinc_LRP1 super family cl31126
putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain ...
377-412 4.59e-03

putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain found in plants. Arabidopsis thaliana has at least 10 distinct members. Proteins containing this domain, including LRP1, generally share the same size, about 300 amino acids, and architecture. This 43-residue domain, and a more C-terminal companion domain of similar size, appear as tightly conserved islands of sequence similarity. The remainder consists largely of low-complexity sequence. Several animal proteins have regions with matching patterns of Cys, Gly, and His residues. These are not included in the model but score between trusted and noise cutoffs.


The actual alignment was detected with superfamily member TIGR01623:

Pssm-ID: 130684  Cd Length: 43  Bit Score: 34.88  E-value: 4.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 578832039  377 KCDQCGNPKGNRCVFSLCRGCCKKRAsketADCPGH 412
Cdd:TIGR01623   1 VCQDCGNQAKKECLFERCRTCCKSRG----FHCVTH 32
 
Name Accession Description Interval E-value
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
18-233 3.78e-91

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: 275.91  E-value: 3.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  18 RHVVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVRDANYRKENLYCevCPEDRPLIVQFCANDPEVFVQAALLAQD 97
Cdd:cd02801    1 KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTR--NPEERPLIVQLGGSDPETLAEAAKIVEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  98 -YCDAIDLNLGCPQMIAKR-----VLLAH------------EKLSVPVTCKIRVFPEID-KTVRYAQMLEKAGCQLLTVH 158
Cdd:cd02801   79 lGADGIDLNMGCPSPKVTKggagaALLKDpelvaeivravrEAVPIPVTVKIRLGWDDEeETLELAKALEDAGASALTVH 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578832039 159 GRTKEQKgpLSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPALFEGRSPAVW 233
Cdd:cd02801  159 GRTREQR--YSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
20-292 1.65e-71

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: 228.36  E-value: 1.65e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039   20 VVAPMVDQSELAWRLLSRRHGAQ-LCYTPMLHAQVFVRDANYRKENLYCEvcPEDRPLIVQFCANDPEVFVQAALLAQD- 97
Cdd:pfam01207   1 LLAPMAGVTDLPFRRLVREYGAGdLVYTEMVTAKAQLRPEKVRIRMLSEL--EEPTPLAVQLGGSDPALLAEAAKLVEDr 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039   98 YCDAIDLNLGCPQMIAKR-----VLLA------------HEKLSVPVTCKIRVF--PEIDKTVRYAQMLEKAGCQLLTVH 158
Cdd:pfam01207  79 GADGIDINMGCPSKKVTRggggaALLRnpdlvaqivkavVKAVGIPVTVKIRIGwdDSHENAVEIAKIVEDAGAQALTVH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  159 GRTKEQKGplSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPALFEGRSPAVWELAE- 237
Cdd:pfam01207 159 GRTRAQNY--EGTADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAEQHTVKTGEFGp 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578832039  238 -----EYLDIVREH-PC---------PLSYVRAHLFklWH-HTLQVHQELREELAKVKTLEGIAAVSQELK 292
Cdd:pfam01207 237 spplaEEAEKVLRHlPYleeflgedkGLRHARKHLA--WYlKGFPGAAELRRELNDVFDPVEALINLDAAL 305
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
20-287 1.82e-62

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: 204.94  E-value: 1.82e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  20 VVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVRDAnyRKENLYCEVCPEDRPLIVQFCANDPEVFVQAALLAQDY- 98
Cdd:COG0042   10 ILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGN--RKTRRLLDFDPEEHPVAVQLFGSDPEELAEAARIAEELg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  99 CDAIDLNLGCPqmiAKRV--------LLAHEKL------------SVPVTCKIR--------VFPEIdktvryAQMLEKA 150
Cdd:COG0042   88 ADEIDINMGCP---VKKVtkggagaaLLRDPELvaeivkavveavDVPVTVKIRlgwddddeNALEF------ARIAEDA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 151 GCQLLTVHGRTKEQ--KGPlsgaASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPALF--- 225
Cdd:COG0042  159 GAAALTVHGRTREQryKGP----ADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFrei 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578832039 226 ----EGRSPA------VWELAEEYLDIVREH---PCPLSYVRAHLFKLWHHtLQVHQELREELAKVKTLEGIAAV 287
Cdd:COG0042  235 daylAGGEAPppsleeVLELLLEHLELLLEFygeRRGLRRMRKHLLWYFKG-LPGARELRRRLSKAKSLAELLEL 308
PRK10415 PRK10415
tRNA-dihydrouridine synthase B; Provisional
18-268 9.32e-23

tRNA-dihydrouridine synthase B; Provisional


Pssm-ID: 182440  Cd Length: 321  Bit Score: 98.50  E-value: 9.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  18 RHVVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVrdanYRKENLYCEVCPEDRPLI--VQFCANDPEVFVQAALL- 94
Cdd:PRK10415  11 RLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQV----WESDKSRLRMVHIDEPGIrtVQIAGSDPKEMADAARIn 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  95 AQDYCDAIDLNLGCP-----QMIAKRVLLAHEKL------------SVPVTCKIRV--FPEIDKTVRYAQMLEKAGCQLL 155
Cdd:PRK10415  87 VESGAQIIDINMGCPakkvnRKLAGSALLQYPDLvksiltevvnavDVPVTLKIRTgwAPEHRNCVEIAQLAEDCGIQAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 156 TVHGRTKeqKGPLSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNlhnpalfEGRsPAVWEL 235
Cdd:PRK10415 167 TIHGRTR--ACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAA-------QGR-PWIFRE 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 578832039 236 AEEYLDIVR-EHPCPLSYVRaHLfkLWHHTLQVH 268
Cdd:PRK10415 237 IQHYLDTGElLPPLPLAEVK-RL--LCAHVRELH 267
put_zinc_LRP1 TIGR01623
putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain ...
377-412 4.59e-03

putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain found in plants. Arabidopsis thaliana has at least 10 distinct members. Proteins containing this domain, including LRP1, generally share the same size, about 300 amino acids, and architecture. This 43-residue domain, and a more C-terminal companion domain of similar size, appear as tightly conserved islands of sequence similarity. The remainder consists largely of low-complexity sequence. Several animal proteins have regions with matching patterns of Cys, Gly, and His residues. These are not included in the model but score between trusted and noise cutoffs.


Pssm-ID: 130684  Cd Length: 43  Bit Score: 34.88  E-value: 4.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 578832039  377 KCDQCGNPKGNRCVFSLCRGCCKKRAsketADCPGH 412
Cdd:TIGR01623   1 VCQDCGNQAKKECLFERCRTCCKSRG----FHCVTH 32
DUF702 pfam05142
Domain of unknown function (DUF702); Members of this family are found in various putative zinc ...
378-412 5.06e-03

Domain of unknown function (DUF702); Members of this family are found in various putative zinc finger proteins.


Pssm-ID: 461560 [Multi-domain]  Cd Length: 154  Bit Score: 37.35  E-value: 5.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 578832039  378 CDQCGNPKGNRCVFSLCRGCCKKRAsketADCPGH 412
Cdd:pfam05142   5 CQDCGNQAKKDCPHMRCRTCCKSRG----FDCPTH 35
 
Name Accession Description Interval E-value
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
18-233 3.78e-91

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: 275.91  E-value: 3.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  18 RHVVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVRDANYRKENLYCevCPEDRPLIVQFCANDPEVFVQAALLAQD 97
Cdd:cd02801    1 KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTR--NPEERPLIVQLGGSDPETLAEAAKIVEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  98 -YCDAIDLNLGCPQMIAKR-----VLLAH------------EKLSVPVTCKIRVFPEID-KTVRYAQMLEKAGCQLLTVH 158
Cdd:cd02801   79 lGADGIDLNMGCPSPKVTKggagaALLKDpelvaeivravrEAVPIPVTVKIRLGWDDEeETLELAKALEDAGASALTVH 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578832039 159 GRTKEQKgpLSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPALFEGRSPAVW 233
Cdd:cd02801  159 GRTREQR--YSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
20-292 1.65e-71

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: 228.36  E-value: 1.65e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039   20 VVAPMVDQSELAWRLLSRRHGAQ-LCYTPMLHAQVFVRDANYRKENLYCEvcPEDRPLIVQFCANDPEVFVQAALLAQD- 97
Cdd:pfam01207   1 LLAPMAGVTDLPFRRLVREYGAGdLVYTEMVTAKAQLRPEKVRIRMLSEL--EEPTPLAVQLGGSDPALLAEAAKLVEDr 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039   98 YCDAIDLNLGCPQMIAKR-----VLLA------------HEKLSVPVTCKIRVF--PEIDKTVRYAQMLEKAGCQLLTVH 158
Cdd:pfam01207  79 GADGIDINMGCPSKKVTRggggaALLRnpdlvaqivkavVKAVGIPVTVKIRIGwdDSHENAVEIAKIVEDAGAQALTVH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  159 GRTKEQKGplSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPALFEGRSPAVWELAE- 237
Cdd:pfam01207 159 GRTRAQNY--EGTADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAEQHTVKTGEFGp 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578832039  238 -----EYLDIVREH-PC---------PLSYVRAHLFklWH-HTLQVHQELREELAKVKTLEGIAAVSQELK 292
Cdd:pfam01207 237 spplaEEAEKVLRHlPYleeflgedkGLRHARKHLA--WYlKGFPGAAELRRELNDVFDPVEALINLDAAL 305
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
20-287 1.82e-62

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: 204.94  E-value: 1.82e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  20 VVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVRDAnyRKENLYCEVCPEDRPLIVQFCANDPEVFVQAALLAQDY- 98
Cdd:COG0042   10 ILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGN--RKTRRLLDFDPEEHPVAVQLFGSDPEELAEAARIAEELg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  99 CDAIDLNLGCPqmiAKRV--------LLAHEKL------------SVPVTCKIR--------VFPEIdktvryAQMLEKA 150
Cdd:COG0042   88 ADEIDINMGCP---VKKVtkggagaaLLRDPELvaeivkavveavDVPVTVKIRlgwddddeNALEF------ARIAEDA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 151 GCQLLTVHGRTKEQ--KGPlsgaASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPALF--- 225
Cdd:COG0042  159 GAAALTVHGRTREQryKGP----ADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFrei 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578832039 226 ----EGRSPA------VWELAEEYLDIVREH---PCPLSYVRAHLFKLWHHtLQVHQELREELAKVKTLEGIAAV 287
Cdd:COG0042  235 daylAGGEAPppsleeVLELLLEHLELLLEFygeRRGLRRMRKHLLWYFKG-LPGARELRRRLSKAKSLAELLEL 308
PRK10415 PRK10415
tRNA-dihydrouridine synthase B; Provisional
18-268 9.32e-23

tRNA-dihydrouridine synthase B; Provisional


Pssm-ID: 182440  Cd Length: 321  Bit Score: 98.50  E-value: 9.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  18 RHVVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVrdanYRKENLYCEVCPEDRPLI--VQFCANDPEVFVQAALL- 94
Cdd:PRK10415  11 RLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQV----WESDKSRLRMVHIDEPGIrtVQIAGSDPKEMADAARIn 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  95 AQDYCDAIDLNLGCP-----QMIAKRVLLAHEKL------------SVPVTCKIRV--FPEIDKTVRYAQMLEKAGCQLL 155
Cdd:PRK10415  87 VESGAQIIDINMGCPakkvnRKLAGSALLQYPDLvksiltevvnavDVPVTLKIRTgwAPEHRNCVEIAQLAEDCGIQAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 156 TVHGRTKeqKGPLSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNlhnpalfEGRsPAVWEL 235
Cdd:PRK10415 167 TIHGRTR--ACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAA-------QGR-PWIFRE 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 578832039 236 AEEYLDIVR-EHPCPLSYVRaHLfkLWHHTLQVH 268
Cdd:PRK10415 237 IQHYLDTGElLPPLPLAEVK-RL--LCAHVRELH 267
PRK10550 PRK10550
tRNA dihydrouridine(16) synthase DusC;
18-224 5.13e-15

tRNA dihydrouridine(16) synthase DusC;


Pssm-ID: 236713  Cd Length: 312  Bit Score: 75.62  E-value: 5.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  18 RHVVAPM--VDQSeLAWRLLSRRHGAQLCYTPMLHaqvfVRDANYRKENLYcEVCPEDR---------PLIVQFCANDPE 86
Cdd:PRK10550   2 RVLLAPMegVLDS-LVRELLTEVNDYDLCITEFLR----VVDQLLPVKVFH-RLCPELHnasrtpsgtLVRIQLLGQYPQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  87 VFVQAALLAQDYCD-AIDLNLGCPQMIAK-----RVLLAHEKL--------------SVPVTCKIRV-FPEIDKTVRYAQ 145
Cdd:PRK10550  76 WLAENAARAVELGSwGVDLNCGCPSKTVNgsgggATLLKDPELiyqgakamreavpaHLPVTVKVRLgWDSGERKFEIAD 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578832039 146 MLEKAGCQLLTVHGRTKEQkGPLSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPAL 224
Cdd:PRK10550 156 AVQQAGATELVVHGRTKED-GYRAEHINWQAIGEIRQRLTIPVIANGEIWDWQSAQQCMAITGCDAVMIGRGALNIPNL 233
PRK11815 PRK11815
tRNA dihydrouridine(20/20a) synthase DusA;
21-269 3.71e-14

tRNA dihydrouridine(20/20a) synthase DusA;


Pssm-ID: 236991 [Multi-domain]  Cd Length: 333  Bit Score: 73.24  E-value: 3.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  21 VAPMVDqselaW---------RLLSRRhgAQLcYTPMLHAQVFVRDANYR--KENlycevcPEDRPLIVQFCANDPEVFV 89
Cdd:PRK11815  15 VAPMMD-----WtdrhcryfhRLLSRH--ALL-YTEMVTTGAIIHGDRERllAFD------PEEHPVALQLGGSDPADLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  90 QAALLAQDY-CDAIDLNLGCPqmiAKRV--------LLAHEKL------------SVPVTCKIRVfpEIDKTVRYAQMLE 148
Cdd:PRK11815  81 EAAKLAEDWgYDEINLNVGCP---SDRVqngrfgacLMAEPELvadcvkamkdavSIPVTVKHRI--GIDDQDSYEFLCD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 149 ------KAGCQLLTVHGRtkeqKGPLSGAASWE-------------HIKAVRKAVAIPVfaNGNIQCLQDVERCLRDtgV 209
Cdd:PRK11815 156 fvdtvaEAGCDTFIVHAR----KAWLKGLSPKEnreippldydrvyRLKRDFPHLTIEI--NGGIKTLEEAKEHLQH--V 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578832039 210 QGVM---SAegnLHNPALFEGRSPAVWELAEEYLDI--VREHPCPlsYVRAHL---FKLWH---HTLQVHQ 269
Cdd:PRK11815 228 DGVMigrAA---YHNPYLLAEVDRELFGEPAPPLSRseVLEAMLP--YIERHLaqgGRLNHitrHMLGLFQ 293
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
126-224 3.49e-09

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: 57.97  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 126 PVTCKI---RVFPE---IDKTVRYAQMLEKAGCQLLTVHGRTKEQKGPLSG------AASWEHIKAVRKAVAIPVFANGN 193
Cdd:cd02803  210 PVGVRLsadDFVPGgltLEEAIEIAKALEEAGVDALHVSGGSYESPPPIIPppyvpeGYFLELAEKIKKAVKIPVIAVGG 289
                         90       100       110
                 ....*....|....*....|....*....|.
gi 578832039 194 IQCLQDVERCLRDTGVQGVMSAEGNLHNPAL 224
Cdd:cd02803  290 IRDPEVAEEILAEGKADLVALGRALLADPDL 320
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
73-200 1.75e-05

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: 46.39  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  73 DRPLIVQFCANDPEVFVQ-AALLAQDYCDAIDLNLGCP-------------QMIAKRVLLAHEKLSVPVTCKIRvfPEID 138
Cdd:cd04740   89 GTPVIASIAGSTVEEFVEvAEKLADAGADAIELNISCPnvkgggmafgtdpEAVAEIVKAVKKATDVPVIVKLT--PNVT 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 139 KTVRYAQMLEKAGCQLL----TVHG-----RTKE-----QKGPLSGAAswehIK--AVR------KAVAIPVFANGNIQC 196
Cdd:cd04740  167 DIVEIARAAEEAGADGLtlinTLKGmaidiETRKpilgnVTGGLSGPA----IKpiALRmvyqvyKAVEIPIIGVGGIAS 242

                 ....
gi 578832039 197 LQDV 200
Cdd:cd04740  243 GEDA 246
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
137-224 5.62e-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: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 137 IDKTVRYAQMLEKAGCQLLTV----HGRTKEQKGPLSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGV 212
Cdd:COG1902  235 LEESVELAKALEEAGVDYLHVssggYEPDAMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLV 314
                         90
                 ....*....|..
gi 578832039 213 MSAEGNLHNPAL 224
Cdd:COG1902  315 ALGRPLLADPDL 326
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
73-226 1.41e-03

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: 40.42  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039  73 DRPLIVQFCANDPEVFVQ-AALLAQDYCDAIDLNLGCPQMIAKRVLL------------AHEKLSVPVTCKIRVFPEIDK 139
Cdd:cd02810   98 GQPLIASVGGSSKEDYVElARKIERAGAKALELNLSCPNVGGGRQLGqdpeavanllkaVKAAVDIPLLVKLSPYFDLED 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 140 TVRYAQMLEKAGCQLLTVHGRT--------------KEQKGPLSGAA----SWEHIKAVRKAVA--IPVFANGNIQCLQD 199
Cdd:cd02810  178 IVELAKAAERAGADGLTAINTIsgrvvdlktvgpgpKRGTGGLSGAPirplALRWVARLAARLQldIPIIGVGGIDSGED 257
                        170       180
                 ....*....|....*....|....*...
gi 578832039 200 VERCLrDTGVQGVMSAEGN-LHNPALFE 226
Cdd:cd02810  258 VLEML-MAGASAVQVATALmWDGPDVIR 284
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
120-205 3.34e-03

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 38.71  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832039 120 HEKLSVPVTCKIRVFPEidktVRYAQmleKAGCQLL--TVHGRTKEQKGPLSgaASWEHIKAVRKAVAIPVFANGNIQCL 197
Cdd:cd04729  119 HEEYNCLLMADISTLEE----ALNAA---KLGFDIIgtTLSGYTEETAKTED--PDFELLKELRKALGIPVIAEGRINSP 189

                 ....*...
gi 578832039 198 QDVERCLR 205
Cdd:cd04729  190 EQAAKALE 197
put_zinc_LRP1 TIGR01623
putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain ...
377-412 4.59e-03

putative zinc finger domain, LRP1 type; This model represents a putative zinc finger domain found in plants. Arabidopsis thaliana has at least 10 distinct members. Proteins containing this domain, including LRP1, generally share the same size, about 300 amino acids, and architecture. This 43-residue domain, and a more C-terminal companion domain of similar size, appear as tightly conserved islands of sequence similarity. The remainder consists largely of low-complexity sequence. Several animal proteins have regions with matching patterns of Cys, Gly, and His residues. These are not included in the model but score between trusted and noise cutoffs.


Pssm-ID: 130684  Cd Length: 43  Bit Score: 34.88  E-value: 4.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 578832039  377 KCDQCGNPKGNRCVFSLCRGCCKKRAsketADCPGH 412
Cdd:TIGR01623   1 VCQDCGNQAKKECLFERCRTCCKSRG----FHCVTH 32
DUF702 pfam05142
Domain of unknown function (DUF702); Members of this family are found in various putative zinc ...
378-412 5.06e-03

Domain of unknown function (DUF702); Members of this family are found in various putative zinc finger proteins.


Pssm-ID: 461560 [Multi-domain]  Cd Length: 154  Bit Score: 37.35  E-value: 5.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 578832039  378 CDQCGNPKGNRCVFSLCRGCCKKRAsketADCPGH 412
Cdd:pfam05142   5 CQDCGNQAKKDCPHMRCRTCCKSRG----FDCPTH 35
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
144-212 7.84e-03

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 37.84  E-value: 7.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578832039 144 AQMLEKAGCQ--LLTVHGRTKEQKGPlsgaaSWEHIKAVRKAVAIPVFANGNIQCLQDVERcLRDTGVQGV 212
Cdd:cd04732  152 AKRFEELGVKaiIYTDISRDGTLSGP-----NFELYKELAAATGIPVIASGGVSSLDDIKA-LKELGVAGV 216
 
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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