|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
34-317 |
5.27e-133 |
|
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: 380.36 E-value: 5.27e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTFQLAA-CAHFYDVSQLGAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDHYLVD 112
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEeLSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 113 ELPKLKKLGALVITNVAGHSDEDYAQVVEKLADSAADMLEINVSCPNVTHGGMSVGTDPVALHRLIKRLRAMTDKPMIVK 192
Cdd:cd04740 81 LLPWLREFGTPVIASIAGSTVEEFVEVAEKLADAGADAIELNISCPNVKGGGMAFGTDPEAVAEIVKAVKKATDVPVIVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 193 MTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQA----------- 261
Cdd:cd04740 161 LTPNVTDIVEIARAAEEAGADGLTLINTLKGMAIDIETRKPILGNVTGGLSGPAIKPIALRMVYQVYKAveipiigvggi 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490234718 262 MpdipiigiggidSGEKALEYLYAGANAVEVGAAALVDPTAPIRIARELDDLLDSR 317
Cdd:cd04740 241 A------------SGEDALEFLMAGASAVQVGTANFVDPEAFKEIIEGLEAYLDEE 284
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
34-315 |
3.22e-126 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 363.32 E-value: 3.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTFQL-AACAHFYDVSQLGAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDHYLVD 112
Cdd:PRK07259 3 SVELPGLKLKNPVMPASGTFGFgGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 113 ELPKLKKLGALVITNVAGHSDEDYAQVVEKLADS-AADMLEINVSCPNVTHGGMSVGTDPVALHRLIKRLRAMTDKPMIV 191
Cdd:PRK07259 83 ELPWLEEFDTPIIANVAGSTEEEYAEVAEKLSKApNVDAIELNISCPNVKHGGMAFGTDPELAYEVVKAVKEVVKVPVIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 192 KMTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQA---------- 261
Cdd:PRK07259 163 KLTPNVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRKPILANVTGGLSGPAIKPIALRMVYQVYQAvdipiigmgg 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490234718 262 -MpdipiigiggidSGEKALEYLYAGANAVEVGAAALVDPTAPIRIARELDDLLD 315
Cdd:PRK07259 243 iS------------SAEDAIEFIMAGASAVQVGTANFYDPYAFPKIIEGLEAYLD 285
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
34-317 |
5.01e-113 |
|
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: 329.34 E-value: 5.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTFQL-AACAHFYDVSQLGAICTKGVSPVPWEGNPSPRTAE--SPSGMVNAVGLQNPGVDHYL 110
Cdd:COG0167 3 SVELAGLKFPNPVGLASGFFDKnAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRlpEDSGLINRMGLNNPGVDAFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 111 vDELPKLKKLGALVITNVAGHSDEDYAQVVEKLADSAADMLEINVSCPNVTHGGMSVGTDPVALHRLIKRLRAMTDKPMI 190
Cdd:COG0167 83 -ERLLPAKRYDVPVIVNIGGNTVEDYVELARRLADAGADYLELNISCPNTPGGGRALGQDPEALAELLAAVKAATDKPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 191 VKMTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQA--------- 261
Cdd:COG0167 162 VKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEAGGLSGPALKPIALRMVREVAQAvggdipiig 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490234718 262 ----MpdipiigiggidSGEKALEYLYAGANAVEVGAAALVD-PTAPIRIARELDDLLDSR 317
Cdd:COG0167 242 vggiS------------TAEDALEFILAGASAVQVGTALFYEgPGLVRRIIRGLEAYLEEK 290
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
34-317 |
3.41e-97 |
|
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.
Pssm-ID: 130109 [Multi-domain] Cd Length: 300 Bit Score: 289.33 E-value: 3.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTF-QLAACAHFYDVSQLGAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDHYLVD 112
Cdd:TIGR01037 2 EVELFGIRFKNPLILASGIMgSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 113 ELPKLKKLGALVITNVAGHSDEDYAQVVEKL--ADSAADMLEINVSCPNVTHGGMSVGTDPVALHRLIKRLRAMTDKPMI 190
Cdd:TIGR01037 82 LKPVREEFPTPLIASVYGSSVEEFAEVAEKLekAPPYVDAYELNLSCPHVKGGGIAIGQDPELSADVVKAVKDKTDVPVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 191 VKMTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQaMPDIPIIGI 270
Cdd:TIGR01037 162 AKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPILANKTGGLSGPAIKPIALRMVYDVYK-MVDIPIIGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490234718 271 GGIDSGEKALEYLYAGANAVEVGAAALVDPTAPIRIARELDDLLDSR 317
Cdd:TIGR01037 241 GGITSFEDALEFLMAGASAVQVGTAVYYRGFAFKKIIEGLIAFLKAE 287
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
34-314 |
7.42e-74 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 229.54 E-value: 7.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTFQLAAC-AHFYDVSQLGAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDHYLVD 112
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEaLKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 113 ELPKLKKLGAL---VITNVAGHSDEDYAQVVEKLADSaADMLEINVSCPNvTHGGMSVGTDPVALHRLIKRLRAMTDKPM 189
Cdd:pfam01180 83 LLKRRKEYPRPdlgINLSKAGMTVDDYVEVARKIGPF-ADYIELNVSCPN-TPGLRALQTDPELAAILLKVVKEVSKVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 190 IVKMTPNVTDIVSICKAAVDAGADALSMIN----TLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQAMPDI 265
Cdd:pfam01180 161 LVKLAPDLTDIVIIDIADVALGEDGLDGINatntTVRGMRIDLKTEKPILANGTGGLSGPPIKPIALKVIRELYQRTGPE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490234718 266 PIIGIG-GIDSGEKALEYLYAGANAVEVGAA-ALVDPTAPIRIARELDDLL 314
Cdd:pfam01180 241 IPIIGVgGIESGEDALEKILAGASAVQIGTAlIFGGPFIFPKIIDELPELL 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
34-317 |
5.27e-133 |
|
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: 380.36 E-value: 5.27e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTFQLAA-CAHFYDVSQLGAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDHYLVD 112
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEeLSRVADLGKLGAIVTKSITLEPREGNPPPRVVETPGGMLNAIGLQNPGVEAFLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 113 ELPKLKKLGALVITNVAGHSDEDYAQVVEKLADSAADMLEINVSCPNVTHGGMSVGTDPVALHRLIKRLRAMTDKPMIVK 192
Cdd:cd04740 81 LLPWLREFGTPVIASIAGSTVEEFVEVAEKLADAGADAIELNISCPNVKGGGMAFGTDPEAVAEIVKAVKKATDVPVIVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 193 MTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQA----------- 261
Cdd:cd04740 161 LTPNVTDIVEIARAAEEAGADGLTLINTLKGMAIDIETRKPILGNVTGGLSGPAIKPIALRMVYQVYKAveipiigvggi 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490234718 262 MpdipiigiggidSGEKALEYLYAGANAVEVGAAALVDPTAPIRIARELDDLLDSR 317
Cdd:cd04740 241 A------------SGEDALEFLMAGASAVQVGTANFVDPEAFKEIIEGLEAYLDEE 284
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
34-315 |
3.22e-126 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 363.32 E-value: 3.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTFQL-AACAHFYDVSQLGAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDHYLVD 112
Cdd:PRK07259 3 SVELPGLKLKNPVMPASGTFGFgGEYARFYDLNGLGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 113 ELPKLKKLGALVITNVAGHSDEDYAQVVEKLADS-AADMLEINVSCPNVTHGGMSVGTDPVALHRLIKRLRAMTDKPMIV 191
Cdd:PRK07259 83 ELPWLEEFDTPIIANVAGSTEEEYAEVAEKLSKApNVDAIELNISCPNVKHGGMAFGTDPELAYEVVKAVKEVVKVPVIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 192 KMTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQA---------- 261
Cdd:PRK07259 163 KLTPNVTDIVEIAKAAEEAGADGLSLINTLKGMAIDIKTRKPILANVTGGLSGPAIKPIALRMVYQVYQAvdipiigmgg 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490234718 262 -MpdipiigiggidSGEKALEYLYAGANAVEVGAAALVDPTAPIRIARELDDLLD 315
Cdd:PRK07259 243 iS------------SAEDAIEFIMAGASAVQVGTANFYDPYAFPKIIEGLEAYLD 285
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
34-317 |
5.01e-113 |
|
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: 329.34 E-value: 5.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTFQL-AACAHFYDVSQLGAICTKGVSPVPWEGNPSPRTAE--SPSGMVNAVGLQNPGVDHYL 110
Cdd:COG0167 3 SVELAGLKFPNPVGLASGFFDKnAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRlpEDSGLINRMGLNNPGVDAFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 111 vDELPKLKKLGALVITNVAGHSDEDYAQVVEKLADSAADMLEINVSCPNVTHGGMSVGTDPVALHRLIKRLRAMTDKPMI 190
Cdd:COG0167 83 -ERLLPAKRYDVPVIVNIGGNTVEDYVELARRLADAGADYLELNISCPNTPGGGRALGQDPEALAELLAAVKAATDKPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 191 VKMTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQA--------- 261
Cdd:COG0167 162 VKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRAIDLETRRPVLANEAGGLSGPALKPIALRMVREVAQAvggdipiig 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490234718 262 ----MpdipiigiggidSGEKALEYLYAGANAVEVGAAALVD-PTAPIRIARELDDLLDSR 317
Cdd:COG0167 242 vggiS------------TAEDALEFILAGASAVQVGTALFYEgPGLVRRIIRGLEAYLEEK 290
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
34-317 |
3.41e-97 |
|
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.
Pssm-ID: 130109 [Multi-domain] Cd Length: 300 Bit Score: 289.33 E-value: 3.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTF-QLAACAHFYDVSQLGAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDHYLVD 112
Cdd:TIGR01037 2 EVELFGIRFKNPLILASGIMgSGVESLRRIDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 113 ELPKLKKLGALVITNVAGHSDEDYAQVVEKL--ADSAADMLEINVSCPNVTHGGMSVGTDPVALHRLIKRLRAMTDKPMI 190
Cdd:TIGR01037 82 LKPVREEFPTPLIASVYGSSVEEFAEVAEKLekAPPYVDAYELNLSCPHVKGGGIAIGQDPELSADVVKAVKDKTDVPVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 191 VKMTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQaMPDIPIIGI 270
Cdd:TIGR01037 162 AKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKPILANKTGGLSGPAIKPIALRMVYDVYK-MVDIPIIGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490234718 271 GGIDSGEKALEYLYAGANAVEVGAAALVDPTAPIRIARELDDLLDSR 317
Cdd:TIGR01037 241 GGITSFEDALEFLMAGASAVQVGTAVYYRGFAFKKIIEGLIAFLKAE 287
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
34-314 |
7.42e-74 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 229.54 E-value: 7.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGTFQLAAC-AHFYDVSQLGAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDHYLVD 112
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEaLKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 113 ELPKLKKLGAL---VITNVAGHSDEDYAQVVEKLADSaADMLEINVSCPNvTHGGMSVGTDPVALHRLIKRLRAMTDKPM 189
Cdd:pfam01180 83 LLKRRKEYPRPdlgINLSKAGMTVDDYVEVARKIGPF-ADYIELNVSCPN-TPGLRALQTDPELAAILLKVVKEVSKVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 190 IVKMTPNVTDIVSICKAAVDAGADALSMIN----TLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRVRQAMPDI 265
Cdd:pfam01180 161 LVKLAPDLTDIVIIDIADVALGEDGLDGINatntTVRGMRIDLKTEKPILANGTGGLSGPPIKPIALKVIRELYQRTGPE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490234718 266 PIIGIG-GIDSGEKALEYLYAGANAVEVGAA-ALVDPTAPIRIARELDDLL 314
Cdd:pfam01180 241 IPIIGVgGIESGEDALEKILAGASAVQIGTAlIFGGPFIFPKIIDELPELL 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
35-309 |
3.81e-53 |
|
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: 176.39 E-value: 3.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 35 TKVAGVEWKNMVGTASG----TFQLAACAHFydvSQLGAICTKGVSPVPWEGNPSPR---------TAESPSGMVNAVGL 101
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGpllkTGELIARAAA---AGFGAVVYKTVTLHPRPGNPLPRvarlppegeSYPEQLGILNSFGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 102 QNPGVDHYLVDELPKLKKL-GALVITNVAGHSDEDYAQVVEKLADSAADMLEINVSCPNVTHGGmSVGTDPVALHRLIKR 180
Cdd:cd02810 78 PNLGLDVWLQDIAKAKKEFpGQPLIASVGGSSKEDYVELARKIERAGAKALELNLSCPNVGGGR-QLGQDPEAVANLLKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 181 LRAMTDKPMIVKMTPNVT--DIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRTGGVSGPAIFPIGLGFVWRV 258
Cdd:cd02810 157 VKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDLKTVGPGPKRGTGGLSGAPIRPLALRWVARL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490234718 259 RQAMPDIPIIGIGG-IDSGEKALEYLYAGANAVEVGAAALVD-PTAPIRIARE 309
Cdd:cd02810 237 AARLQLDIPIIGVGgIDSGEDVLEMLMAGASAVQVATALMWDgPDVIRKIKKE 289
|
|
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
34-296 |
3.05e-36 |
|
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: 132.41 E-value: 3.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASG--TFQLAACAHFYDVSQLGAIcTKGVSP-VPWEGNPSPRTAESPSGMVNAVGLQN------- 103
Cdd:cd02940 3 SVTFCGIKFPNPFGLASAppTTSYPMIRRAFEAGWGGAV-TKTLGLdKDIVTNVSPRIARLRTSGRGQIGFNNielisek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 104 PGvdHYLVDELPKLKK---LGALVITNVAGHSDEDYAQVVEKLADSAADMLEINVSCPnvtHG------GMSVGTDPVAL 174
Cdd:cd02940 82 PL--EYWLKEIRELKKdfpDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCP---HGmpergmGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 175 HRLIKRLRAMTDKPMIVKMTPNVTDIVSICKAAVDAGADALSMINT---LVGLRIDIRTGEPIIANRT--GGVSGPAIFP 249
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTvnsLMGVDLDGTPPAPGVEGKTtyGGYSGPAVKP 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490234718 250 IGLGFVWRVRQAMPDIPIIGIG-GIDSGEKALEYLYAGANAVEVGAAA 296
Cdd:cd02940 237 IALRAVSQIARAPEPGLPISGIgGIESWEDAAEFLLLGASVVQVCTAV 284
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
34-314 |
3.11e-32 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 121.98 E-value: 3.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGTASGtfqlAACAHFYDVSQL-----GAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDH 108
Cdd:PRK02506 3 STQIAGFKFDNCLMNAAG----VYCMTKEELEEVeasaaGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 109 YLvDELPKLKKLGAL--VITNVAGHSDEDYAQVVEKLADSA-ADMLEINVSCPNVThGGMSVGTDPVALHRLIKRLRAMT 185
Cdd:PRK02506 79 YL-DYVLELQKKGPNkpHFLSVVGLSPEETHTILKKIQASDfNGLVELNLSCPNVP-GKPQIAYDFETTEQILEEVFTYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 186 DKPMIVKMTPNVtDIVSICKAAVDAGADALSMINTL----VGLRIDIRTGEPII--ANRTGGVSGPAIFPIGLGFVWRVR 259
Cdd:PRK02506 157 TKPLGVKLPPYF-DIVHFDQAAAIFNKFPLAFVNCInsigNGLVIDPEDETVVIkpKNGFGGIGGDYIKPTALANVRAFY 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490234718 260 QAMPDIPIIGIG-GIDSGEKALEYLYAGANAVEVGAAALVD-PTAPIRIARELDDLL 314
Cdd:PRK02506 236 QRLNPSIQIIGTgGVKTGRDAFEHILCGASMVQVGTALHKEgPAVFERLTKELKAIM 292
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
34-310 |
9.02e-28 |
|
Dihydroorotate dehydrogenase (DHOD) class 2. 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, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.
Pssm-ID: 240089 Cd Length: 327 Bit Score: 110.28 E-value: 9.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGtasgtfqLAA-----CAHFYDVSQLGA----ICTkgVSPVPWEGNPSPRTAESPS--GMVNAVGLQ 102
Cdd:cd04738 40 EVEVFGLTFPNPVG-------LAAgfdknAEAIDALLALGFgfveVGT--VTPRPQPGNPKPRLFRLPEdeALINRMGFN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 103 NPGVDhYLVDELPKLKKLGALVITNVAGHSD-------EDYAQVVEKLADsAADMLEINVSCPNvTHGGMSVgTDPVALH 175
Cdd:cd04738 111 NDGAD-AVAKRLKKRRPRGGPLGVNIGKNKDtpledavEDYVIGVRKLGP-YADYLVVNVSSPN-TPGLRDL-QGKEALR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 176 RLIKRLRAMTD-----KPMIVKMTPNVTD--IVSICKAAVDAGADALSMINTLVGlridiRTG--EPIIANRTGGVSGPA 246
Cdd:cd04738 187 ELLTAVKEERNklgkkVPLLVKIAPDLSDeeLEDIADVALEHGVDGIIATNTTIS-----RPGllRSPLANETGGLSGAP 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490234718 247 IFPIGLGFVWRVRQAMPDIPI-IGIGGIDSGEKALEYLYAGANAVEVgAAALV--DPTAPIRIAREL 310
Cdd:cd04738 262 LKERSTEVLRELYKLTGGKIPiIGVGGISSGEDAYEKIRAGASLVQL-YTGLVyeGPGLVKRIKREL 327
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
112-298 |
8.95e-27 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 109.26 E-value: 8.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 112 DELPKLKKL---GALVITNVAGHSDEDYAQVVEKLADSAADMLEINVSCPnvtHG----GM--SVGTDPVALHRLIKRLR 182
Cdd:PRK08318 88 REIRRVKRDypdRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCP---HGmserGMgsAVGQVPELVEMYTRWVK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 183 AMTDKPMIVKMTPNVTDIVSICKAAVDAGADALSMINT---LVGLRIDIRTGEPIIANRT--GGVSGPAIFPIGLGFVWR 257
Cdd:PRK08318 165 RGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTinsITGVDLDRMIPMPIVNGKSshGGYCGPAVKPIALNMVAE 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490234718 258 VRQAmpdipIIGIGGIDSG-------EKALEYLYAGANAVEVGAAALV 298
Cdd:PRK08318 245 IARD-----PETRGLPISGiggietwRDAAEFILLGAGTVQVCTAAMQ 287
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
65-314 |
4.65e-24 |
|
Dihydroorotate dehydrogenase (DHOD) class 1A 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: 240092 Cd Length: 294 Bit Score: 99.71 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 65 SQLGAICTKGVSPVPWEGNPSPRTAESPSGMVNAVGLQNPGVDHYL------VDELPKLKKlgALVITnVAGhSDEDYAQ 138
Cdd:cd04741 32 SSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLeyirtiSDGLPGSAK--PFFIS-VTG-SAEDIAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 139 VVEKLADSA---ADMLEINVSCPNVThGGMSVGTDPVALHRLIKRLRAMTDKPMIVKMTPnVTDIV--SICKAAVDAGAD 213
Cdd:cd04741 108 MYKKIAAHQkqfPLAMELNLSCPNVP-GKPPPAYDFDATLEYLTAVKAAYSIPVGVKTPP-YTDPAqfDTLAEALNAFAC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 214 ALSMI---NTL-VGLRIDIRTGEPII--ANRTGGVSGPAIFPIGLGFVWRVRQAMPDIPIIGIGG-IDSGEKALEYLYAG 286
Cdd:cd04741 186 PISFItatNTLgNGLVLDPERETVVLkpKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQIIGVGgVLDGRGAFRMRLAG 265
|
250 260
....*....|....*....|....*....
gi 490234718 287 ANAVEVGAA-ALVDPTAPIRIARELDDLL 314
Cdd:cd04741 266 ASAVQVGTAlGKEGPKVFARIEKELEDIW 294
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
34-315 |
3.96e-21 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 92.15 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 34 STKVAGVEWKNMVGtasgtfqLAA-----CAHFYDVSQLG----AICTkgVSPVPWEGNPSPR-----TAESpsgMVNAV 99
Cdd:PRK05286 50 PVTVMGLTFPNPVG-------LAAgfdknGEAIDALGALGfgfvEVGT--VTPRPQPGNPKPRlfrlpEDEA---LINRM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 100 GLQNPGVDHyLVDELPKLKK---LGA-LVITNVAGHSD--EDYAQVVEKLADSAaDMLEINVSCPNvTHGGMSVgTDPVA 173
Cdd:PRK05286 118 GFNNDGADA-LAERLKKAYRgipLGInIGKNKDTPLEDavDDYLICLEKLYPYA-DYFTVNISSPN-TPGLRDL-QYGEA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 174 LHRLIKRLRAMTD-----KPMIVKMTPNVTD--IVSICKAAVDAGADALSMINTLVGlridiRTG--EPIIANRTGGVSG 244
Cdd:PRK05286 194 LDELLAALKEAQAelhgyVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIATNTTLS-----RDGlkGLPNADEAGGLSG 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490234718 245 PAIFPIGLGFVWRVRQAMPDIPI-IGIGGIDSGEKALEYLYAGANAVEVgAAALV--DPTAPIRIARELDDLLD 315
Cdd:PRK05286 269 RPLFERSTEVIRRLYKELGGRLPiIGVGGIDSAEDAYEKIRAGASLVQI-YSGLIyeGPGLVKEIVRGLARLLR 341
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
136-292 |
3.02e-19 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 87.59 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 136 YAQVVEKLADSAADMLEINVSCPnvtHG------GMSVGTDPVALHRLIKRLRAMTDKPMIVKMTPNVTDIVSICKAAVD 209
Cdd:PLN02495 129 WEEIIERVEETGVDALEINFSCP---HGmperkmGAAVGQDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 210 AGADALSMINTL---VGLRIDIRTGEPIIANRT--GGVSGPAIFPIGLGFVWRVRQAMPDIPIIGIGGI-----DSGEKA 279
Cdd:PLN02495 206 SGCEGVAAINTImsvMGINLDTLRPEPCVEGYStpGGYSSKAVRPIALAKVMAIAKMMKSEFPEDRSLSgiggvETGGDA 285
|
170
....*....|...
gi 490234718 280 LEYLYAGANAVEV 292
Cdd:PLN02495 286 AEFILLGADTVQV 298
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
37-292 |
1.47e-15 |
|
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273408 Cd Length: 335 Bit Score: 76.36 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 37 VAGVEWKNMVGTASGTFQLAACAHFYDVSQLGAICTKGVSPVPWEGNPSPRTAESPS--GMVNAVGLQNPGVDhYLVDEL 114
Cdd:TIGR01036 50 VLGLKFPNPLGLAAGFDKDGEAIDALGAMGFGFLEIGTVTPKPQPGNPRPRLFRLIEdeALINRMGFNNHGAD-VLVERL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 115 PKLKKLGALVItNV-------AGHSDEDYAQVVEKLAdSAADMLEINVSCPNVThgGMSVGTDPVALHRLIKRLRAMTDK 187
Cdd:TIGR01036 129 KRARYKGPIGI-NIgknkdtpSEDAKEDYAACLRKLG-PLADYLVVNVSSPNTP--GLRDLQYKAELRDLLTAVKQEQDG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 188 -------PMIVKMTPNVT--DIVSICKAAVDAGADALSMINTLVGLriDIRTGePIIANRTGGVSGPAIFPIGLGFVWRV 258
Cdd:TIGR01036 205 lrrvhrvPVLVKIAPDLTesDLEDIADSLVELGIDGVIATNTTVSR--SLVQG-PKNSDETGGLSGKPLQDKSTEIIRRL 281
|
250 260 270
....*....|....*....|....*....|....*
gi 490234718 259 RQAMPDIPI-IGIGGIDSGEKALEYLYAGANAVEV 292
Cdd:TIGR01036 282 YAELQGRLPiIGVGGISSAQDALEKIRAGASLLQI 316
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
103-317 |
1.39e-07 |
|
Dihydroorotate dehydrogenase (DHOD) like proteins. 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. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.
Pssm-ID: 240090 Cd Length: 325 Bit Score: 52.23 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 103 NPGVDHYLvDELPKLKKLGAL-VITNVAGHSDE---DYAQVVEklaDSAADMLEINVscpnvthggMSVGTDPV------ 172
Cdd:cd04739 81 NLGPEEYL-ELIRRAKRAVSIpVIASLNGVSAGgwvDYARQIE---EAGADALELNI---------YALPTDPDisgaev 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 173 -ALH-RLIKRLRAMTDKPMIVKMTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRtggVSGPAifPI 250
Cdd:cd04739 148 eQRYlDILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRFYQPDIDLETLEVVPNLL---LSSPA--EI 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490234718 251 GLGFVW------RVRqampdIPIIGIGGIDSGEKALEYLYAGANAVEVgAAALVDPTAPI--RIARELDDLLDSR 317
Cdd:cd04739 223 RLPLRWiailsgRVK-----ASLAASGGVHDAEDVVKYLLAGADVVMT-TSALLRHGPDYigTLLAGLEAWMEEH 291
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
75-314 |
8.04e-07 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 50.12 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 75 VSPVPWEGNPSPRTAESPS--GMVNAVGLQNPGVD------------HYLVDELPKLKKLGALVITNVAGH--------- 131
Cdd:PLN02826 116 VTPLPQPGNPKPRVFRLREegAIINRYGFNSEGIVavakrlgaqhgkRKLDETSSSSFSSDDVKAGGKAGPgilgvnlgk 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 132 ---SD---EDYAQVVEKLAdSAADMLEINVSCPNVTHGGMSVGTDPvaLHRLIKRLRAMTDK---------PMIVKMTPN 196
Cdd:PLN02826 196 nktSEdaaADYVQGVRALS-QYADYLVINVSSPNTPGLRKLQGRKQ--LKDLLKKVLAARDEmqwgeegppPLLVKIAPD 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 197 VT--DIVSICKAAVDAGADALSMINTLVGLRIDIRTGEpiIANRTGGVSGPAIFPIGLGFVWR-VRQAMPDIPIIGIGGI 273
Cdd:PLN02826 273 LSkeDLEDIAAVALALGIDGLIISNTTISRPDSVLGHP--HADEAGGLSGKPLFDLSTEVLREmYRLTRGKIPLVGCGGV 350
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490234718 274 DSGEKALEYLYAGANAVEVGAAALVDPTAPI-RIARELDDLL 314
Cdd:PLN02826 351 SSGEDAYKKIRAGASLVQLYTAFAYEGPALIpRIKAELAACL 392
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
107-215 |
4.10e-06 |
|
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: 47.71 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 107 DHYLVDELPKLKKLGaLVITNVAGHSDEDYAQVVEKLADSAADMLEINVSCP--NVTHGGM--SVGTDPVALHRLIKRLR 182
Cdd:pfam01207 40 EKVRIRMLSELEEPT-PLAVQLGGSDPALLAEAAKLVEDRGADGIDINMGCPskKVTRGGGgaALLRNPDLVAQIVKAVV 118
|
90 100 110
....*....|....*....|....*....|....*..
gi 490234718 183 AMTDKPMIVKMT----PNVTDIVSICKAAVDAGADAL 215
Cdd:pfam01207 119 KAVGIPVTVKIRigwdDSHENAVEIAKIVEDAGAQAL 155
|
|
| arch_FMN |
cd02911 |
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ... |
109-237 |
3.54e-05 |
|
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: 44.24 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 109 YLVDELPKLKKLGALVITNVAGHSDEDYAQVVEKLADsAADMLEINVSC--PNVThggmSVGTDPVALH---RLIKRLRA 183
Cdd:cd02911 60 FIEGEIKALKDSNVLVGVNVRSSSLEPLLNAAALVAK-NAAILEINAHCrqPEMV----EAGAGEALLKdpeRLSEFIKA 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490234718 184 M--TDKPMIVKMTPNVT-DIVSICKAAVDAGADAL-------SMINTLVGLRiDIRTGEPIIAN 237
Cdd:cd02911 135 LkeTGVPVSVKIRAGVDvDDEELARLIEKAGADIIhvdamdpGNHADLKKIR-DISTELFIIGN 197
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
105-317 |
1.08e-04 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 43.32 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 105 GVDHYLvDELPKLKKLGAL-VITNVAGHSDE---DYAQVVEklaDSAADMLEINVscpnvthggMSVGTDPV-------A 173
Cdd:PRK07565 85 GPEEYL-ELIRRAKEAVDIpVIASLNGSSAGgwvDYARQIE---QAGADALELNI---------YYLPTDPDisgaeveQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 174 LH-RLIKRLRAMTDKPMIVKMTPNVTDIVSICKAAVDAGADALSMINTLVGLRIDIRTGEPIIANRtggVSGPAIfpIGL 252
Cdd:PRK07565 152 RYlDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRFYQPDIDLETLEVVPGLV---LSTPAE--LRL 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490234718 253 GFVWrvrQAMPDIPIIGIGGIDSG----EKALEYLYAGANAVEVgAAALVDPTAPI--RIARELDDLLDSR 317
Cdd:PRK07565 227 PLRW---IAILSGRVGADLAATTGvhdaEDVIKMLLAGADVVMI-ASALLRHGPDYigTILRGLEDWMERH 293
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
129-215 |
1.41e-04 |
|
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: 43.16 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490234718 129 AGHSDEDYAQVVEKLADSAADMLEINVSCP--NVTHGG-----MSvgtDPVALHRLIKRLRAMTDKPMIVKM----TPNV 197
Cdd:COG0042 69 FGSDPEELAEAARIAEELGADEIDINMGCPvkKVTKGGagaalLR---DPELVAEIVKAVVEAVDVPVTVKIrlgwDDDD 145
|
90
....*....|....*...
gi 490234718 198 TDIVSICKAAVDAGADAL 215
Cdd:COG0042 146 ENALEFARIAEDAGAAAL 163
|
|
| |
