|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
1-321 |
0e+00 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 689.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 1 MRIGQYQLKNCLIAAPMAGITDRPFRSLCYKMGAGMTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMA 80
Cdd:PRK10415 1 MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSDPKEMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 81 AAAKINVANGAQIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSPEERNCVKIAQLAEH 160
Cdd:PRK10415 81 DAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCVEIAQLAED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 161 CGIQALAIHGRTRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREIQHY 240
Cdd:PRK10415 161 CGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 241 LATGELLSPMPIGEVQHLMNEHIQELHDFYGPSKGARIARKHVSWYLREHAPDDQFRRTFNTIEDASEQLEVLGAYFENF 320
Cdd:PRK10415 241 LDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENF 320
|
.
gi 499461065 321 A 321
Cdd:PRK10415 321 A 321
|
|
| nifR3_yhdG |
TIGR00737 |
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
3-321 |
0e+00 |
|
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: 511.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 3 IGQYQLKNCLIAAPMAGITDRPFRSLCYKMGAGMTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMAAA 82
Cdd:TIGR00737 1 IGNIQLKSRVVLAPMAGVTDSPFRRLVAEYGAGLTVCEMVSSEAIVYDSQRTMRLLDIAEDETPISVQLFGSDPDTMAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 83 AKINVANGAQIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSPEERNCVKIAQLAEHCG 162
Cdd:TIGR00737 81 AKINEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAVDIPVTVKIRIGWDDAHINAVEAARIAEDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 163 IQALAIHGRTRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREIQHYLA 242
Cdd:TIGR00737 161 AQAVTLHGRTRAQGYSGEANWDIIARVKQAVRIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEQYLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499461065 243 TGELLSPMPIGEVQHLMNEHIQELHDFYGPSKGARIARKHVSWYLREHAPDDQFRRTFNTIEDASEQLEVLGAYFENFA 321
Cdd:TIGR00737 241 TGKYKPPPTFAEKLDAILRHLQLLADYYGESKGLRIARKHIAWYLKGFPGNAALRQTLNHASSFQEVKQLLDDFFETVG 319
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
4-313 |
4.02e-160 |
|
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: 449.16 E-value: 4.02e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 4 GQYQLKNCLIAAPMAGITDRPFRSLCYKMGAGMTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMAAAA 83
Cdd:COG0042 1 GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFGSDPEELAEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 84 KINVANGAQIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSPEERNCVKIAQLAEHCGI 163
Cdd:COG0042 81 RIAEELGADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLGWDDDDENALEFARIAEDAGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 164 QALAIHGRTRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREIQHYLAT 243
Cdd:COG0042 161 AALTVHGRTREQRYKGPADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYLAG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 244 GElLSPMPIGEVQHLMNEHIQELHDFYGPSKGARIARKHVSWYLREHAPDDQFRRTFNTIEDASEQLEVL 313
Cdd:COG0042 241 GE-APPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELL 309
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
13-320 |
2.24e-143 |
|
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: 406.71 E-value: 2.24e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 13 IAAPMAGITDRPFRSLCYKMGAG-MTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMAAAAKINVANGA 91
Cdd:pfam01207 1 LLAPMAGVTDLPFRRLVREYGAGdLVYTEMVTAKAQLRPEKVRIRMLSELEEPTPLAVQLGGSDPALLAEAAKLVEDRGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 92 QIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSPEERNCVKIAQLAEHCGIQALAIHGR 171
Cdd:pfam01207 81 DGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHENAVEIAKIVEDAGAQALTVHGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 172 TRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREiQHYLATGELLSPMP 251
Cdd:pfam01207 161 TRAQNYEGTADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAE-QHTVKTGEFGPSPP 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499461065 252 IGEVQHLMNEHIQELHDFYGPSKGARIARKHVSWYLREHAPDDQFRRTFNTIEDASEQLEVLGAYFENF 320
Cdd:pfam01207 240 LAEEAEKVLRHLPYLEEFLGEDKGLRHARKHLAWYLKGFPGAAELRRELNDVFDPVEALINLDAALRAA 308
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
12-241 |
5.05e-109 |
|
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: 316.36 E-value: 5.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 12 LIAAPMAGITDRPFRSLCYKMGAGMTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMAAAAKINVANGA 91
Cdd:cd02801 2 LILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTRNPEERPLIVQLGGSDPETLAEAAKIVEELGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 92 QIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSpEERNCVKIAQLAEHCGIQALAIHGR 171
Cdd:cd02801 82 DGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGWD-DEEETLELAKALEDAGASALTVHGR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 172 TRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREIQHYL 241
Cdd:cd02801 161 TREQRYSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELL 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
1-321 |
0e+00 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 689.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 1 MRIGQYQLKNCLIAAPMAGITDRPFRSLCYKMGAGMTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMA 80
Cdd:PRK10415 1 MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSDPKEMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 81 AAAKINVANGAQIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSPEERNCVKIAQLAEH 160
Cdd:PRK10415 81 DAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCVEIAQLAED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 161 CGIQALAIHGRTRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREIQHY 240
Cdd:PRK10415 161 CGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 241 LATGELLSPMPIGEVQHLMNEHIQELHDFYGPSKGARIARKHVSWYLREHAPDDQFRRTFNTIEDASEQLEVLGAYFENF 320
Cdd:PRK10415 241 LDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENF 320
|
.
gi 499461065 321 A 321
Cdd:PRK10415 321 A 321
|
|
| nifR3_yhdG |
TIGR00737 |
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
3-321 |
0e+00 |
|
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: 511.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 3 IGQYQLKNCLIAAPMAGITDRPFRSLCYKMGAGMTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMAAA 82
Cdd:TIGR00737 1 IGNIQLKSRVVLAPMAGVTDSPFRRLVAEYGAGLTVCEMVSSEAIVYDSQRTMRLLDIAEDETPISVQLFGSDPDTMAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 83 AKINVANGAQIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSPEERNCVKIAQLAEHCG 162
Cdd:TIGR00737 81 AKINEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAVDIPVTVKIRIGWDDAHINAVEAARIAEDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 163 IQALAIHGRTRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREIQHYLA 242
Cdd:TIGR00737 161 AQAVTLHGRTRAQGYSGEANWDIIARVKQAVRIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEQYLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499461065 243 TGELLSPMPIGEVQHLMNEHIQELHDFYGPSKGARIARKHVSWYLREHAPDDQFRRTFNTIEDASEQLEVLGAYFENFA 321
Cdd:TIGR00737 241 TGKYKPPPTFAEKLDAILRHLQLLADYYGESKGLRIARKHIAWYLKGFPGNAALRQTLNHASSFQEVKQLLDDFFETVG 319
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
4-313 |
4.02e-160 |
|
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: 449.16 E-value: 4.02e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 4 GQYQLKNCLIAAPMAGITDRPFRSLCYKMGAGMTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMAAAA 83
Cdd:COG0042 1 GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFGSDPEELAEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 84 KINVANGAQIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSPEERNCVKIAQLAEHCGI 163
Cdd:COG0042 81 RIAEELGADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLGWDDDDENALEFARIAEDAGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 164 QALAIHGRTRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREIQHYLAT 243
Cdd:COG0042 161 AALTVHGRTREQRYKGPADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYLAG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 244 GElLSPMPIGEVQHLMNEHIQELHDFYGPSKGARIARKHVSWYLREHAPDDQFRRTFNTIEDASEQLEVL 313
Cdd:COG0042 241 GE-APPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELL 309
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
13-320 |
2.24e-143 |
|
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: 406.71 E-value: 2.24e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 13 IAAPMAGITDRPFRSLCYKMGAG-MTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMAAAAKINVANGA 91
Cdd:pfam01207 1 LLAPMAGVTDLPFRRLVREYGAGdLVYTEMVTAKAQLRPEKVRIRMLSELEEPTPLAVQLGGSDPALLAEAAKLVEDRGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 92 QIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSPEERNCVKIAQLAEHCGIQALAIHGR 171
Cdd:pfam01207 81 DGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHENAVEIAKIVEDAGAQALTVHGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 172 TRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREiQHYLATGELLSPMP 251
Cdd:pfam01207 161 TRAQNYEGTADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAE-QHTVKTGEFGPSPP 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499461065 252 IGEVQHLMNEHIQELHDFYGPSKGARIARKHVSWYLREHAPDDQFRRTFNTIEDASEQLEVLGAYFENF 320
Cdd:pfam01207 240 LAEEAEKVLRHLPYLEEFLGEDKGLRHARKHLAWYLKGFPGAAELRRELNDVFDPVEALINLDAALRAA 308
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
12-241 |
5.05e-109 |
|
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: 316.36 E-value: 5.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 12 LIAAPMAGITDRPFRSLCYKMGAGMTVSEMLSSNPQVWKTDKSRLRMVHSDEPGIRSVQIAGSDPDEMAAAAKINVANGA 91
Cdd:cd02801 2 LILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTRNPEERPLIVQLGGSDPETLAEAAKIVEELGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 92 QIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWSpEERNCVKIAQLAEHCGIQALAIHGR 171
Cdd:cd02801 82 DGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGWD-DEEETLELAKALEDAGASALTVHGR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 172 TRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRPWIFREIQHYL 241
Cdd:cd02801 161 TREQRYSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELL 230
|
|
| PRK10550 |
PRK10550 |
tRNA dihydrouridine(16) synthase DusC; |
69-289 |
2.58e-31 |
|
tRNA dihydrouridine(16) synthase DusC;
Pssm-ID: 236713 Cd Length: 312 Bit Score: 119.53 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 69 VQIAGSDPDEMAAAAKINVANGAQIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAV--DVPVTLKIRTGWSP 146
Cdd:PRK10550 67 IQLLGQYPQWLAENAARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVTVKVRLGWDS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 147 EERNcVKIAQLAEHCGIQALAIHGRTRSCLFNGEA-EYDNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGR 225
Cdd:PRK10550 147 GERK-FEIADAVQQAGATELVVHGRTKEDGYRAEHiNWQAIGEIRQRLTIPVIANGEIWDWQSAQQCMAITGCDAVMIGR 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499461065 226 AAQGRPWIFREIQHYLAtgellsPMPIGEVQHLMNEHIQ-ELHDFYGPSKGARIARkhvsW--YLRE 289
Cdd:PRK10550 226 GALNIPNLSRVVKYNEP------RMPWPEVVALLQKYTRlEKQGDTGLYHVARIKQ----WlgYLRK 282
|
|
| PRK11815 |
PRK11815 |
tRNA dihydrouridine(20/20a) synthase DusA; |
15-284 |
5.12e-22 |
|
tRNA dihydrouridine(20/20a) synthase DusA;
Pssm-ID: 236991 [Multi-domain] Cd Length: 333 Bit Score: 94.43 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 15 APMAGITDRPFR---------SLCYkmgagmtvSEMLSSnPQVWKTDKSRLRMVHSDEPGIrSVQIAGSDPDEMAAAAKI 85
Cdd:PRK11815 16 APMMDWTDRHCRyfhrllsrhALLY--------TEMVTT-GAIIHGDRERLLAFDPEEHPV-ALQLGGSDPADLAEAAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 86 NVANGAQIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIRTGWS---PEERNCVKIAQLAEHcG 162
Cdd:PRK11815 86 AEDWGYDEINLNVGCPSDRVQNGRFGACLMAEPELVADCVKAMKDAVSIPVTVKHRIGIDdqdSYEFLCDFVDTVAEA-G 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 163 IQALAIHGRTrsclfngeA----------------EYDNIRTVKQ-----TVAIpviaNGDITDPLKARAVLEYtgADAL 221
Cdd:PRK11815 165 CDTFIVHARK--------AwlkglspkenreipplDYDRVYRLKRdfphlTIEI----NGGIKTLEEAKEHLQH--VDGV 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499461065 222 MIGRAAQGRPWIFREIQHYLaTGELLSPMPIGEVQHLMNEHIQE-------LHD--------FYGpSKGARIARKHVS 284
Cdd:PRK11815 231 MIGRAAYHNPYLLAEVDREL-FGEPAPPLSRSEVLEAMLPYIERhlaqggrLNHitrhmlglFQG-LPGARAWRRYLS 306
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
34-237 |
1.65e-17 |
|
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: 81.25 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 34 AGMTVSEMLSS-NPQVWKTDKSRLRMVHSDEPGIRSVQiaGSDPDEMAAAAKINVANGAQIIDINMGCPAKKVNRKLags 112
Cdd:cd02810 69 LGILNSFGLPNlGLDVWLQDIAKAKKEFPGQPLIASVG--GSSKEDYVELARKIERAGAKALELNLSCPNVGGGRQL--- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 113 alLRYPELVEKILSAVVNAVDVPVTLKIrtGWSPEERNCVKIAQLAEHCGIQALAIHGRTRSCLFNGE------------ 180
Cdd:cd02810 144 --GQDPEAVANLLKAVKAAVDIPLLVKL--SPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKtvgpgpkrgtgg 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 181 --------AEYDNIRTVKQTVA--IPVIANGDITdplKARAVLEY--TGADALMIGRAAQGR-PWIFREI 237
Cdd:cd02810 220 lsgapirpLALRWVARLAARLQldIPIIGVGGID---SGEDVLEMlmAGASAVQVATALMWDgPDVIRKI 286
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
69-237 |
9.06e-15 |
|
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: 73.35 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 69 VQIAGSDPDEMAAAAKINVANGAQIIDINMGCPakkvNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIrtgwSPEE 148
Cdd:cd04740 94 ASIAGSTVEEFVEVAEKLADAGADAIELNISCP----NVKGGGMAFGTDPEAVAEIVKAVKKATDVPVIVKL----TPNV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 149 RNCVKIAQLAEHCG---------IQALAIHGRTRS-CLFNG--------------EAEYDnirtVKQTVAIPVIANGDIT 204
Cdd:cd04740 166 TDIVEIARAAEEAGadgltlintLKGMAIDIETRKpILGNVtgglsgpaikpialRMVYQ----VYKAVEIPIIGVGGIA 241
|
170 180 190
....*....|....*....|....*....|....*
gi 499461065 205 DplkARAVLEY--TGADALMIGRAAQGRPWIFREI 237
Cdd:cd04740 242 S---GEDALEFlmAGASAVQVGTANFVDPEAFKEI 273
|
|
| arch_FMN |
cd02911 |
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ... |
15-237 |
1.73e-13 |
|
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent flavin oxidoreductase (oxidored) FMN-binding family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN. The specific function of this group is unknown.
Pssm-ID: 239237 [Multi-domain] Cd Length: 233 Bit Score: 68.89 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 15 APMAGITDRPF-RSLCYKMGAG-----------MTVS---------EMLSSNP------QVWKTDKSRLRMvhsdepgir 67
Cdd:cd02911 5 ASMAGITDGDFcRKRADHAGLVflggynldertIEAArklvkrgrkEFLPDDPlefiegEIKALKDSNVLV--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 68 SVQIAGSDPDEMAAAAKINVANGAqIIDINMGCPAKKVNRKLAGSALLRYPELVEKILSAVvNAVDVPVTLKIRTGWSPE 147
Cdd:cd02911 76 GVNVRSSSLEPLLNAAALVAKNAA-ILEINAHCRQPEMVEAGAGEALLKDPERLSEFIKAL-KETGVPVSVKIRAGVDVD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 148 ErncVKIAQLAEHCGiqALAIHgrTRSCLFNGEAEYDNIRTVkqTVAIPVIANGDITDPLKARAVLEYtGADALMIGRAA 227
Cdd:cd02911 154 D---EELARLIEKAG--ADIIH--VDAMDPGNHADLKKIRDI--STELFIIGNNSVTTIESAKEMFSY-GADMVSVARAS 223
|
250
....*....|
gi 499461065 228 qgRPWIFREI 237
Cdd:cd02911 224 --LPENIEWL 231
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
69-237 |
2.41e-13 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 69.41 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 69 VQIAGSDPDEMAAAA-KINVANGAQIIDINMGCPakkvNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIrtgwSPE 147
Cdd:PRK07259 96 ANVAGSTEEEYAEVAeKLSKAPNVDAIELNISCP----NVKHGGMAFGTDPELAYEVVKAVKEVVKVPVIVKL----TPN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 148 ERNCVKIAQLAEHCGIQAL---------AIHGRTRSCLFN-------GEA--------EYDnirtVKQTVAIPVIANGDI 203
Cdd:PRK07259 168 VTDIVEIAKAAEEAGADGLslintlkgmAIDIKTRKPILAnvtgglsGPAikpialrmVYQ----VYQAVDIPIIGMGGI 243
|
170 180 190
....*....|....*....|....*....|....*.
gi 499461065 204 TDplkARAVLEY--TGADALMIGRAAQGRPWIFREI 237
Cdd:PRK07259 244 SS---AEDAIEFimAGASAVQVGTANFYDPYAFPKI 276
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
69-237 |
1.16e-12 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 67.02 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 69 VQIAGSDPDEMAAAAKInVAN-GAQIIDINMGCPakkvNRKLAGSALLRYPELVEKILSAVVNAVDVPVTLKIrtgwSPE 147
Cdd:COG0167 97 VNIGGNTVEDYVELARR-LADaGADYLELNISCP----NTPGGGRALGQDPEALAELLAAVKAATDKPVLVKL----APD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 148 ERNCVKIAQLAEHCGIQAL---------AIHGRTRSCLFNGEA---------EY--DNIRTVKQTVA--IPVIANGDITD 205
Cdd:COG0167 168 LTDIVEIARAAEEAGADGViainttlgrAIDLETRRPVLANEAgglsgpalkPIalRMVREVAQAVGgdIPIIGVGGIST 247
|
170 180 190
....*....|....*....|....*....|....*
gi 499461065 206 plkARAVLEYT--GADALMIGRAA-QGRPWIFREI 237
Cdd:COG0167 248 ---AEDALEFIlaGASAVQVGTALfYEGPGLVRRI 279
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
120-227 |
8.75e-11 |
|
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: 61.82 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 120 LVEKILSAVVNAV--DVPVTLKI------RTGWSPEErnCVKIAQLAEHCGIQALAIHGRT--------RSCLFNGEAEY 183
Cdd:cd02803 193 FLLEIVAAVREAVgpDFPVGVRLsaddfvPGGLTLEE--AIEIAKALEEAGVDALHVSGGSyespppiiPPPYVPEGYFL 270
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 499461065 184 DNIRTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAA 227
Cdd:cd02803 271 ELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRAL 314
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
120-227 |
4.99e-08 |
|
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: 53.63 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 120 LVEkILSAVVNAV--DVPVTLKI------RTGWSPEErnCVKIAQLAEHCGIQALAI-----HGRTRSCLFNGEAEYDNI 186
Cdd:COG1902 202 LLE-VVEAVRAAVgpDFPVGVRLsptdfvEGGLTLEE--SVELAKALEEAGVDYLHVssggyEPDAMIPTIVPEGYQLPF 278
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499461065 187 -RTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAA 227
Cdd:COG1902 279 aARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRPL 320
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
63-237 |
1.65e-06 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 48.88 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 63 EPGIrSVQIAGSDPDEMAAAAKiNVANGAQIIDINMGCPAKKVNRKLAGSallryPELVEKILSAVVNAVDVPVTLKIrt 142
Cdd:pfam01180 94 DLGI-NLSKAGMTVDDYVEVAR-KIGPFADYIELNVSCPNTPGLRALQTD-----PELAAILLKVVKEVSKVPVLVKL-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 143 gwSPEERNCVKIAQLAE---HCGIQALAIHGRTRSCLF-----------------NGEAEYD----NIRTVKQTV--AIP 196
Cdd:pfam01180 165 --APDLTDIVIIDIADValgEDGLDGINATNTTVRGMRidlktekpilangtgglSGPPIKPialkVIRELYQRTgpEIP 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499461065 197 VIANGDITdplKARAVLEY--TGADALMIGRAAQ-GRPWIFREI 237
Cdd:pfam01180 243 IIGVGGIE---SGEDALEKilAGASAVQIGTALIfGGPFIFPKI 283
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
123-235 |
8.52e-06 |
|
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.
Pssm-ID: 239242 [Multi-domain] Cd Length: 336 Bit Score: 46.72 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 123 KILSAVVNAV------DVPVTLKIRT------GWSPEErnCVKIAQ-LAEHcGIQALAIhgrtrSCLFNGEAEYDNI--- 186
Cdd:cd02932 205 RFLLEVVDAVravwpeDKPLFVRISAtdwvegGWDLED--SVELAKaLKEL-GVDLIDV-----SSGGNSPAQKIPVgpg 276
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 499461065 187 ------RTVKQTVAIPVIANGDITDPLKARAVLEYTGADALMIGRAAQGRP-WIFR 235
Cdd:cd02932 277 yqvpfaERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVALGRELLRNPyWPLH 332
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
40-162 |
2.40e-05 |
|
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: 45.35 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 40 EMLSSNP-QVWKTDKSRLRMVHSDEPGIRSVqIAGSDPDEMAAAAKINVANGAQIIDINMGCPAKKVNRKLaGSALLRYP 118
Cdd:cd02940 76 ELISEKPlEYWLKEIRELKKDFPDKILIASI-MCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGM-GAAVGQDP 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 499461065 119 ELVEKILSAVVNAVDVPVTLKIrtgwSPEERNCVKIAQLAEHCG 162
Cdd:cd02940 154 ELVEEICRWVREAVKIPVIAKL----TPNITDIREIARAAKEGG 193
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
69-225 |
7.51e-04 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 39.88 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 69 VQIAGSDPDE--MAAAAKINVAnGAQIIDINMGCPAKkvnrklagsallryPELVEKILSAVVNAV-DVPVTLKIRTGWS 145
Cdd:cd04722 62 VQLAINDAAAavDIAAAAARAA-GADGVEIHGAVGYL--------------AREDLELIRELREAVpDVKVVVKLSPTGE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 146 peernCVKIAQLAEHCGIQALAIHGRTRSCLFNGEAEYDNIRTVKQTVAIPVIANGDITDPLKARAVLEyTGADALMIGR 225
Cdd:cd04722 127 -----LAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALA-LGADGVIVGS 200
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
40-139 |
8.91e-04 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 40.70 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 40 EMLSSNP-QVWKTDKSRLRMVHSDEPGIRSVqIAGSDPDEMAAAAKINVANGAQIIDINMGCPAKKVNRKLaGSALLRYP 118
Cdd:PRK08318 76 ELITDRPlEVNLREIRRVKRDYPDRALIASI-MVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGM-GSAVGQVP 153
|
90 100
....*....|....*....|.
gi 499461065 119 ELVEKILSAVVNAVDVPVTLK 139
Cdd:PRK08318 154 ELVEMYTRWVKRGSRLPVIVK 174
|
|
| MetH2 |
COG1410 |
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ... |
77-136 |
2.38e-03 |
|
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; Methionine synthase I, cobalamin-binding domain is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 441020 [Multi-domain] Cd Length: 1141 Bit Score: 39.55 E-value: 2.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499461065 77 DEMAAAAKINVANGAQIIDINMGCPakkvnrklagsaLLRYPELVEKILSAVVNAVDVPV 136
Cdd:COG1410 358 DEALEVAREQVEAGAQILDVNVDEP------------GRDEVAAMVRFLNLLASEVRVPL 405
|
|
| |
