|
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: 708.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 1 MRIGHHQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMA 80
Cdd:PRK10415 1 MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSDPKEMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 81 AAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEPEHRNCVEIAQLAEE 160
Cdd:PRK10415 81 DAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCVEIAQLAED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 161 CGIQALTIHGRTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHY 240
Cdd:PRK10415 161 CGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 241 LDTGELLPPLPLAEVKRLLCAHVRELHDFYGQAKGYRIARKHVSWYLQEHAPDDQFRRTFNAIEDASEQLEALEAYFENF 320
Cdd:PRK10415 241 LDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENF 320
|
.
gi 1461085473 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: 526.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 3 IGHHQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMAAA 82
Cdd:TIGR00737 1 IGNIQLKSRVVLAPMAGVTDSPFRRLVAEYGAGLTVCEMVSSEAIVYDSQRTMRLLDIAEDETPISVQLFGSDPDTMAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 83 ARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEPEHRNCVEIAQLAEECG 162
Cdd:TIGR00737 81 AKINEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAVDIPVTVKIRIGWDDAHINAVEAARIAEDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 163 IQALTIHGRTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLD 242
Cdd:TIGR00737 161 AQAVTLHGRTRAQGYSGEANWDIIARVKQAVRIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEQYLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1461085473 243 TGELLPPLPLAEVKRLLCAHVRELHDFYGQAKGYRIARKHVSWYLQEHAPDDQFRRTFNAIEDASEQLEALEAYFENFA 321
Cdd:TIGR00737 241 TGKYKPPPTFAEKLDAILRHLQLLADYYGESKGLRIARKHIAWYLKGFPGNAALRQTLNHASSFQEVKQLLDDFFETVG 319
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
4-314 |
8.91e-159 |
|
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: 445.69 E-value: 8.91e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 4 GHHQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMAAAA 83
Cdd:COG0042 1 GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFGSDPEELAEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 84 RINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEPEHRNCVEIAQLAEECGI 163
Cdd:COG0042 81 RIAEELGADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLGWDDDDENALEFARIAEDAGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 164 QALTIHGRTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLDT 243
Cdd:COG0042 161 AALTVHGRTREQRYKGPADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYLAG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1461085473 244 GELLPPlPLAEVKRLLCAHVRELHDFYGQAKGYRIARKHVSWYLQEHAPDDQFRRTFNAIEDASEQLEALE 314
Cdd:COG0042 241 GEAPPP-SLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELLE 310
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
13-320 |
5.60e-152 |
|
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: 428.28 E-value: 5.60e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 13 IAAPMAGITDRPFRTLCYEMGAG-LTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMAAAARINVESGA 91
Cdd:pfam01207 1 LLAPMAGVTDLPFRRLVREYGAGdLVYTEMVTAKAQLRPEKVRIRMLSELEEPTPLAVQLGGSDPALLAEAAKLVEDRGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 92 QIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEPEHRNCVEIAQLAEECGIQALTIHGR 171
Cdd:pfam01207 81 DGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHENAVEIAKIVEDAGAQALTVHGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 172 TRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREiQHYLDTGELLPPLP 251
Cdd:pfam01207 161 TRAQNYEGTADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAE-QHTVKTGEFGPSPP 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1461085473 252 LAEVKRLLCAHVRELHDFYGQAKGYRIARKHVSWYLQEHAPDDQFRRTFNAIEDASEQLEALEAYFENF 320
Cdd:pfam01207 240 LAEEAEKVLRHLPYLEEFLGEDKGLRHARKHLAWYLKGFPGAAELRRELNDVFDPVEALINLDAALRAA 308
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
11-242 |
9.95e-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: 315.97 E-value: 9.95e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 11 RLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMAAAARINVESG 90
Cdd:cd02801 1 KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTRNPEERPLIVQLGGSDPETLAEAAKIVEELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 91 AQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEpEHRNCVEIAQLAEECGIQALTIHG 170
Cdd:cd02801 81 ADGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGWD-DEEETLELAKALEDAGASALTVHG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1461085473 171 RTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLD 242
Cdd:cd02801 160 RTREQRYSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
|
|
| |
|
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: 708.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 1 MRIGHHQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMA 80
Cdd:PRK10415 1 MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSDPKEMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 81 AAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEPEHRNCVEIAQLAEE 160
Cdd:PRK10415 81 DAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCVEIAQLAED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 161 CGIQALTIHGRTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHY 240
Cdd:PRK10415 161 CGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 241 LDTGELLPPLPLAEVKRLLCAHVRELHDFYGQAKGYRIARKHVSWYLQEHAPDDQFRRTFNAIEDASEQLEALEAYFENF 320
Cdd:PRK10415 241 LDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENF 320
|
.
gi 1461085473 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: 526.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 3 IGHHQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMAAA 82
Cdd:TIGR00737 1 IGNIQLKSRVVLAPMAGVTDSPFRRLVAEYGAGLTVCEMVSSEAIVYDSQRTMRLLDIAEDETPISVQLFGSDPDTMAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 83 ARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEPEHRNCVEIAQLAEECG 162
Cdd:TIGR00737 81 AKINEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAVDIPVTVKIRIGWDDAHINAVEAARIAEDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 163 IQALTIHGRTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLD 242
Cdd:TIGR00737 161 AQAVTLHGRTRAQGYSGEANWDIIARVKQAVRIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEQYLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1461085473 243 TGELLPPLPLAEVKRLLCAHVRELHDFYGQAKGYRIARKHVSWYLQEHAPDDQFRRTFNAIEDASEQLEALEAYFENFA 321
Cdd:TIGR00737 241 TGKYKPPPTFAEKLDAILRHLQLLADYYGESKGLRIARKHIAWYLKGFPGNAALRQTLNHASSFQEVKQLLDDFFETVG 319
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
4-314 |
8.91e-159 |
|
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: 445.69 E-value: 8.91e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 4 GHHQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMAAAA 83
Cdd:COG0042 1 GNLELPNPLILAPMAGVTDRPFRRLCRELGAGLLYTEMVSARALLHGNRKTRRLLDFDPEEHPVAVQLFGSDPEELAEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 84 RINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEPEHRNCVEIAQLAEECGI 163
Cdd:COG0042 81 RIAEELGADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIRLGWDDDDENALEFARIAEDAGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 164 QALTIHGRTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLDT 243
Cdd:COG0042 161 AALTVHGRTREQRYKGPADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYLAG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1461085473 244 GELLPPlPLAEVKRLLCAHVRELHDFYGQAKGYRIARKHVSWYLQEHAPDDQFRRTFNAIEDASEQLEALE 314
Cdd:COG0042 241 GEAPPP-SLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELLE 310
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
13-320 |
5.60e-152 |
|
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: 428.28 E-value: 5.60e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 13 IAAPMAGITDRPFRTLCYEMGAG-LTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMAAAARINVESGA 91
Cdd:pfam01207 1 LLAPMAGVTDLPFRRLVREYGAGdLVYTEMVTAKAQLRPEKVRIRMLSELEEPTPLAVQLGGSDPALLAEAAKLVEDRGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 92 QIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEPEHRNCVEIAQLAEECGIQALTIHGR 171
Cdd:pfam01207 81 DGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHENAVEIAKIVEDAGAQALTVHGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 172 TRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREiQHYLDTGELLPPLP 251
Cdd:pfam01207 161 TRAQNYEGTADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAE-QHTVKTGEFGPSPP 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1461085473 252 LAEVKRLLCAHVRELHDFYGQAKGYRIARKHVSWYLQEHAPDDQFRRTFNAIEDASEQLEALEAYFENF 320
Cdd:pfam01207 240 LAEEAEKVLRHLPYLEEFLGEDKGLRHARKHLAWYLKGFPGAAELRRELNDVFDPVEALINLDAALRAA 308
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
11-242 |
9.95e-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: 315.97 E-value: 9.95e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 11 RLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSVPEEMAAAARINVESG 90
Cdd:cd02801 1 KLILAPMVGVTDLPFRLLCRRYGADLVYTEMISAKALLRGNRKRLRLLTRNPEERPLIVQLGGSDPETLAEAAKIVEELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 91 AQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTGWEpEHRNCVEIAQLAEECGIQALTIHG 170
Cdd:cd02801 81 ADGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGWD-DEEETLELAKALEDAGASALTVHG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1461085473 171 RTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLD 242
Cdd:cd02801 160 RTREQRYSGPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
|
|
| PRK10550 |
PRK10550 |
tRNA dihydrouridine(16) synthase DusC; |
11-264 |
1.01e-33 |
|
tRNA dihydrouridine(16) synthase DusC;
Pssm-ID: 236713 Cd Length: 312 Bit Score: 125.69 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 11 RLIAAPMAGITDRPFRTLCYEMGA-GLTVSEMMSSNPQVWESdKSRLRMVHIDEPGIRT-------VQIAGSVPEEMAAA 82
Cdd:PRK10550 2 RVLLAPMEGVLDSLVRELLTEVNDyDLCITEFLRVVDQLLPV-KVFHRLCPELHNASRTpsgtlvrIQLLGQYPQWLAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 83 ARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAV--DVPVTLKIRTGWEPEHRNcVEIAQLAEE 160
Cdd:PRK10550 81 AARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVTVKVRLGWDSGERK-FEIADAVQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 161 CGIQALTIHGRTRACLFNGDA-EYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQH 239
Cdd:PRK10550 160 AGATELVVHGRTKEDGYRAEHiNWQAIGEIRQRLTIPVIANGEIWDWQSAQQCMAITGCDAVMIGRGALNIPNLSRVVKY 239
|
250 260
....*....|....*....|....*
gi 1461085473 240 yldtGEllPPLPLAEVKRLLCAHVR 264
Cdd:PRK10550 240 ----NE--PRMPWPEVVALLQKYTR 258
|
|
| PRK11815 |
PRK11815 |
tRNA dihydrouridine(20/20a) synthase DusA; |
1-308 |
4.43e-24 |
|
tRNA dihydrouridine(20/20a) synthase DusA;
Pssm-ID: 236991 [Multi-domain] Cd Length: 333 Bit Score: 100.21 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 1 MRIGHHQLRNRLIAAPMAGITDRPFR---------TLCYemgagltvSEMMSSnPQVWESDKSRLRMVHIDEPGIrTVQI 71
Cdd:PRK11815 2 PEKMSKLPSRRFSVAPMMDWTDRHCRyfhrllsrhALLY--------TEMVTT-GAIIHGDRERLLAFDPEEHPV-ALQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 72 AGSVPEEMAAAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIRTG---WEPEH 148
Cdd:PRK11815 72 GGSDPADLAEAAKLAEDWGYDEINLNVGCPSDRVQNGRFGACLMAEPELVADCVKAMKDAVSIPVTVKHRIGiddQDSYE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 149 --RNCVEIAQLAeecGIQALTIHGRtRACLfNG------------DaeYDSIRAVKQKV-SIPIIANGDITDPLKARAVL 213
Cdd:PRK11815 152 flCDFVDTVAEA---GCDTFIVHAR-KAWL-KGlspkenreipplD--YDRVYRLKRDFpHLTIEINGGIKTLEEAKEHL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 214 DYtgADALMIGRAAQGRPWIFREIQHYLdTGELLPPLPLAEVKRLLCAHVRE-------LHD--------FYGQaKGYRI 278
Cdd:PRK11815 225 QH--VDGVMIGRAAYHNPYLLAEVDREL-FGEPAPPLSRSEVLEAMLPYIERhlaqggrLNHitrhmlglFQGL-PGARA 300
|
330 340 350
....*....|....*....|....*....|....*
gi 1461085473 279 ARKHVSwylqEH-----APDDQFRRTFNAIEDASE 308
Cdd:PRK11815 301 WRRYLS----ENahkpgAGIEVLEEALALVEEAAL 331
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
30-237 |
1.05e-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: 81.63 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 30 YEMGAGLTVSEMMSS-NPQVWESDKSRLRMVHIDEPGIrtVQIAGSVPEEMAAAARINVESGAQIIDINMGCPAKKVNRK 108
Cdd:cd02810 65 YPEQLGILNSFGLPNlGLDVWLQDIAKAKKEFPGQPLI--ASVGGSSKEDYVELARKIERAGAKALELNLSCPNVGGGRQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 109 LagsalLQYPDQVKSILTAVVNAVDVPVTLKIrtGWEPEHRNCVEIAQLAEECGIQALTIHGRTRACLFNGD-------- 180
Cdd:cd02810 143 L-----GQDPEAVANLLKAVKAAVDIPLLVKL--SPYFDLEDIVELAKAAERAGADGLTAINTISGRVVDLKtvgpgpkr 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1461085473 181 ------------AEYDSIRAVKQ--KVSIPIIANGDITdplKARAVLDY--TGADALMIGRAAQGR-PWIFREI 237
Cdd:cd02810 216 gtgglsgapirpLALRWVARLAArlQLDIPIIGVGGID---SGEDVLEMlmAGASAVQVATALMWDgPDVIRKI 286
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
69-237 |
2.75e-17 |
|
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: 80.67 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 69 VQIAGSVPEEMAAAARINVESGAQIIDINMGCPakkvNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIrtgwEPEH 148
Cdd:cd04740 94 ASIAGSTVEEFVEVAEKLADAGADAIELNISCP----NVKGGGMAFGTDPEAVAEIVKAVKKATDVPVIVKL----TPNV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 149 RNCVEIAQLAEECGIQALT-----------IHGRtRACLFN------GDAeydsIR--------AVKQKVSIPIIANGDI 203
Cdd:cd04740 166 TDIVEIARAAEEAGADGLTlintlkgmaidIETR-KPILGNvtgglsGPA----IKpialrmvyQVYKAVEIPIIGVGGI 240
|
170 180 190
....*....|....*....|....*....|....
gi 1461085473 204 TDPLKARAVLdYTGADALMIGRAAQGRPWIFREI 237
Cdd:cd04740 241 ASGEDALEFL-MAGASAVQVGTANFVDPEAFKEI 273
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
69-237 |
3.83e-14 |
|
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: 71.64 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 69 VQIAGSVPEEMAAAARINVESGAQIIDINMGCPakkvNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLKIrTgwePEH 148
Cdd:COG0167 97 VNIGGNTVEDYVELARRLADAGADYLELNISCP----NTPGGGRALGQDPEALAELLAAVKAATDKPVLVKL-A---PDL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 149 RNCVEIAQLAEECGIQAL----TIHGR------TRACLFN------GDAEYD-SIRAVKQ-----KVSIPIIANGDITDp 206
Cdd:COG0167 169 TDIVEIARAAEEAGADGViainTTLGRaidletRRPVLANeagglsGPALKPiALRMVREvaqavGGDIPIIGVGGIST- 247
|
170 180 190
....*....|....*....|....*....|....
gi 1461085473 207 lkARAVLDYT--GADALMIGRAA-QGRPWIFREI 237
Cdd:COG0167 248 --AEDALEFIlaGASAVQVGTALfYEGPGLVRRI 279
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
61-237 |
5.65e-12 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 65.17 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 61 IDEPGIrtVQIAGSVPEEMAAAA-RINVESGAQIIDINMGCPakkvNRKLAGSALLQYPDQVKSILTAVVNAVDVPVTLK 139
Cdd:PRK07259 90 FDTPII--ANVAGSTEEEYAEVAeKLSKAPNVDAIELNISCP----NVKHGGMAFGTDPELAYEVVKAVKEVVKVPVIVK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 140 IrtgwEPEHRNCVEIAQLAEECGIQALT-----------IHGRtRACLFNGDAEYdSIRAVK-----------QKVSIPI 197
Cdd:PRK07259 164 L----TPNVTDIVEIAKAAEEAGADGLSlintlkgmaidIKTR-KPILANVTGGL-SGPAIKpialrmvyqvyQAVDIPI 237
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1461085473 198 IANGDITDplkARAVLDY--TGADALMIGRAAQGRPWIFREI 237
Cdd:PRK07259 238 IGMGGISS---AEDAIEFimAGASAVQVGTANFYDPYAFPKI 276
|
|
| arch_FMN |
cd02911 |
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ... |
11-237 |
7.92e-12 |
|
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: 63.89 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 11 RLIAAPMAGITDRPFrTLCYEMGAGLTV----------------------SEMMSSNP-QVWESDKSRLRmvhiDEPGIR 67
Cdd:cd02911 1 PVALASMAGITDGDF-CRKRADHAGLVFlggynldertieaarklvkrgrKEFLPDDPlEFIEGEIKALK----DSNVLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 68 TVQIAGSVPEEMAAAARINVESGAqIIDINMGCPAKKVNRKLAGSALLQYPDQVKSILTAVvNAVDVPVTLKIRTGWEPe 147
Cdd:cd02911 76 GVNVRSSSLEPLLNAAALVAKNAA-ILEINAHCRQPEMVEAGAGEALLKDPERLSEFIKAL-KETGVPVSVKIRAGVDV- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 148 hrNCVEIAQLAEECGIQALTIHgrtrACLFNGDAEYDSIRAVKQKvsIPIIANGDITDPLKARAVLDYtGADALMIGRAA 227
Cdd:cd02911 153 --DDEELARLIEKAGADIIHVD----AMDPGNHADLKKIRDISTE--LFIIGNNSVTTIESAKEMFSY-GADMVSVARAS 223
|
250
....*....|
gi 1461085473 228 qgRPWIFREI 237
Cdd:cd02911 224 --LPENIEWL 231
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
2-227 |
5.14e-10 |
|
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: 59.51 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 2 RIGHHQLRNRLIAAPMAG--------ITDRPFRTlcYEM----GAGLTVSEMMSSNPQvwESDKSRLRMVHIDE--PGIR 67
Cdd:cd02803 5 KIGGLTLKNRIVMAPMTEnmatedgtPTDELIEY--YEErakgGVGLIITEAAYVDPE--GKGYPGQLGIYDDEqiPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 68 T-------------VQIA--------------------------GSVPEEM------------AAAARINVESGAQIIDI 96
Cdd:cd02803 81 KlteavhahgakifAQLAhagrqaqpnltggpppapsaipspggGEPPREMtkeeieqiiedfAAAARRAKEAGFDGVEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 97 NMG---------CPAkkVNR---KLAGSA------LLQypdqvksILTAVVNAV--DVPVTLKI------RTGWEPEhrN 150
Cdd:cd02803 161 HGAhgyllsqflSPY--TNKrtdEYGGSLenrarfLLE-------IVAAVREAVgpDFPVGVRLsaddfvPGGLTLE--E 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 151 CVEIAQLAEECGIQALTIHGRT--------RACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYTGADALM 222
Cdd:cd02803 230 AIEIAKALEEAGVDALHVSGGSyespppiiPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVA 309
|
....*
gi 1461085473 223 IGRAA 227
Cdd:cd02803 310 LGRAL 314
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
124-227 |
3.91e-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: 54.02 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 124 ILTAVVNAV--DVPVTLKI------RTGWEPEHrnCVEIAQLAEECGIQAL-----TIHGRTRACLFNGDAEYDSI-RAV 189
Cdd:COG1902 205 VVEAVRAAVgpDFPVGVRLsptdfvEGGLTLEE--SVELAKALEEAGVDYLhvssgGYEPDAMIPTIVPEGYQLPFaARI 282
|
90 100 110
....*....|....*....|....*....|....*...
gi 1461085473 190 KQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAA 227
Cdd:COG1902 283 RKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRPL 320
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
187-235 |
2.15e-05 |
|
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: 45.56 E-value: 2.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1461085473 187 RAVKQKVSIPIIANGDITDPLKARAVLDYTGADALMIGRAAQGRP-WIFR 235
Cdd:cd02932 283 ERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVALGRELLRNPyWPLH 332
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
88-167 |
9.80e-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: 43.43 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 88 ESGAQIIDINMGCPAKKVNRKLaGSALLQYPDQVKSILTAVVNAVDVPVTLKIrtgwEPEHRNCVEIAQLAEECGIQALT 167
Cdd:cd02940 124 EAGADALELNFSCPHGMPERGM-GAAVGQDPELVEEICRWVREAVKIPVIAKL----TPNITDIREIARAAKEGGADGVS 198
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
151-226 |
5.18e-04 |
|
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: 40.64 E-value: 5.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1461085473 151 CVEIAQLAEECG--IQALTIHGRTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDyTGADALMIGRA 226
Cdd:cd04729 132 TLEEALNAAKLGfdIIGTTLSGYTEETAKTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALE-LGADAVVVGSA 208
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
64-226 |
1.81e-03 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 39.12 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 64 PGIRTVQIAGSVPEEMAAAARiNVESGAQIIDINmgcpakkVNRKLAGSALLQYPDQVKSI--------LTAVVNAVDVP 135
Cdd:PRK13585 66 EAIEKIIEAVGVPVQLGGGIR-SAEDAASLLDLG-------VDRVILGTAAVENPEIVRELseefgserVMVSLDAKDGE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 136 VTLKirtGW-EPEHRNCVEIAQLAEECGIQALtihgrtracLF-NGDAE-------YDSIRAVKQKVSIPIIANGDIT-- 204
Cdd:PRK13585 138 VVIK---GWtEKTGYTPVEAAKRFEELGAGSI---------LFtNVDVEgllegvnTEPVKELVDSVDIPVIASGGVTtl 205
|
170 180
....*....|....*....|..
gi 1461085473 205 DPLKAravLDYTGADALMIGRA 226
Cdd:PRK13585 206 DDLRA---LKEAGAAGVVVGSA 224
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
25-225 |
3.01e-03 |
|
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: 38.34 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 25 FRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGI-RTVQIAGS---VPEEMAAAARInvESGAQIIDINMGC 100
Cdd:cd04722 17 LAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLpLGVQLAINdaaAAVDIAAAAAR--AAGADGVEIHGAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1461085473 101 PAKkvnrklagsallqyPDQVKSILTAVVNAV-DVPVTLKIRTGWEpehrncVEIAQLAEECGIQALTIHGRTRACLFNG 179
Cdd:cd04722 95 GYL--------------AREDLELIRELREAVpDVKVVVKLSPTGE------LAAAAAEEAGVDEVGLGNGGGGGGGRDA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1461085473 180 DAEYDSI-RAVKQKVSIPIIANGDITDPLKARAVLdYTGADALMIGR 225
Cdd:cd04722 155 VPIADLLlILAKRGSKVPVIAGGGINDPEDAAEAL-ALGADGVIVGS 200
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
151-226 |
7.69e-03 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 37.05 E-value: 7.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1461085473 151 CVEIAQLAEECGIQ--ALTIHGRTRACLFNGDAEYDSIRAVKQKVSIPIIANGDITDPLKARAVLDYtGADALMIGRA 226
Cdd:PRK01130 128 TLEEGLAAQKLGFDfiGTTLSGYTEETKKPEEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALEL-GAHAVVVGGA 204
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
73-139 |
8.50e-03 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 37.62 E-value: 8.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1461085473 73 GSVPEEMAAAARINVESGAQIIDINMGCPAKKVNRKLaGSALLQYPDQVKSILTAVVNAVDVPVTLK 139
Cdd:PRK08318 109 ECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGM-GSAVGQVPELVEMYTRWVKRGSRLPVIVK 174
|
|
| metH |
PRK09490 |
B12-dependent methionine synthase; Provisional |
83-98 |
9.44e-03 |
|
B12-dependent methionine synthase; Provisional
Pssm-ID: 236539 [Multi-domain] Cd Length: 1229 Bit Score: 37.85 E-value: 9.44e-03
|
| |
