|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
1-343 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 700.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 1 MQTLTITTPDDWHLHFRDNEMLAETVPATARCFQRAIVMPNLVPPVVNAEMAMAYKGRIEAARPKGSSFEPLMTLFLTNQ 80
Cdd:COG0418 2 MQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 81 TTPQDIIDAKQAG-VTACKLYPAGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEVTEHHIDIFDREKVFIDTHLGP 159
Cdd:COG0418 82 TTPEEIARAKASGvVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 160 IVDAFPKLKVVFEHITTADAASFVAGASEFVGATITPQHLLLNRNDLLVGGVRPHNYCLPVLKRNTHQKALRDMVASGNK 239
Cdd:COG0418 162 LRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 240 KFFLGTDSAPHARHKKENACGCAGCYSAWSAIELYAEVFEQLGAIDKLEGFASHYGADFYGLPRNTTTMTLVKESWTVPE 319
Cdd:COG0418 242 KFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPE 321
|
330 340
....*....|....*....|....
gi 1832801142 320 QVTLADGTdMVPFYAGQTLQWKLE 343
Cdd:COG0418 322 SIPFGDDT-LVPFRAGETLNWRVV 344
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
1-344 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 543.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 1 MQTLTITTPDDWHLHFRDNEMLAETVPATARCFQRAIVMPNLVPPVVNAEMAMAYKGRIEAARPKGSSFEPLMTLFLTNQ 80
Cdd:PLN02599 20 GTELTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 81 TTPQDIIDAKQAG-VTACKLYPAGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEVTEHHIDIFDREKVFIDTHLGP 159
Cdd:PLN02599 100 TTPEEIKAAKASGvVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 160 IVDAFPKLKVVFEHITTADAASFVAGASEF-VGATITPQHLLLNRNDLLVGGVRPHNYCLPVLKRNTHQKALRDMVASGN 238
Cdd:PLN02599 180 LVQKLPQLKIVMEHITTMDAVEFVESCGDGnVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 239 KKFFLGTDSAPHARHKKENACGCAGCYSAWSAIELYAEVFEQLGAIDKLEGFASHYGADFYGLPRNTTTMTLVKESWTVP 318
Cdd:PLN02599 260 KKFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVP 339
|
330 340
....*....|....*....|....*.
gi 1832801142 319 EQVTLADGTdMVPFYAGQTLQWKLEK 344
Cdd:PLN02599 340 EAYSFGGGT-VVPMFAGETIPWSVVS 364
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
4-340 |
5.27e-179 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 499.12 E-value: 5.27e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 4 LTITTPDDWHLHFRDNEMLAETVPATARCFQRAIVMPNLVPPVVNAEMAMAYKGRIEAARPkGSSFEPLMTLFLTNQTTP 83
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADP-GPNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 84 QDIIDAKQA-GVTACKLYPAGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEVTEHHIDIFDREKVFIdTHLGPIVD 162
Cdd:cd01294 80 EELREAKKKgGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 163 AFPKLKVVFEHITTADAASFVAGASEFVGATITPQHLLLNRNDLLVGGVRPHNYCLPVLKRNTHQKALRDMVASGNKKFF 242
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 243 LGTDSAPHARHKKENACGCAGCYSAWSAIELYAEVFEQLGAIDKLEGFASHYGADFYGLPRNTTTMTLVKESWTVPEQVT 322
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIP 318
|
330
....*....|....*...
gi 1832801142 323 LADGtDMVPFYAGQTLQW 340
Cdd:cd01294 319 FGNN-GVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
4-342 |
1.62e-158 |
|
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in microbial genomes than a related dihydroorotase that appears in a complex with aspartyltranscarbamoylase or as a homologous domain in multifunctional proteins of pyrimidine biosynthesis in higher eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 129935 Cd Length: 341 Bit Score: 447.34 E-value: 1.62e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 4 LTITTPDDWHLHFRDNEMLAETVPATARCFQRAIVMPNLVPPVVNAEMAMAYKGRIEAARPKGSSFEPLMTLFLTNQTTP 83
Cdd:TIGR00856 2 LTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 84 QDIIDAK-QAGVTACKLYPAGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEVTEHHIDIFDREKVFIDTHLGPIVD 162
Cdd:TIGR00856 82 EELERAKnEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 163 AFPKLKVVFEHITTADAASFVAGASEFVGATITPQHLLLNRNDLLVGGVRPHNYCLPVLKRNTHQKALRDMVASGNKKFF 242
Cdd:TIGR00856 162 RFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKFF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 243 LGTDSAPHARHKKENACGCAGCYSAWSAIELYAEVFEQLGAIDKLEGFASHYGADFYGLPRNTTTMTLVKESWTVPEQVT 322
Cdd:TIGR00856 242 LGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESIA 321
|
330 340
....*....|....*....|
gi 1832801142 323 LADGTdMVPFYAGQTLQWKL 342
Cdd:TIGR00856 322 LTDDT-LVPFRAGETLSWSV 340
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
11-304 |
1.64e-10 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 61.36 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 11 DWHLHFRDNEMLAETVP------ATARCFQRAI--------VMPNLVPPVVNAeMAMAYKG-----RIEAARP---KGSS 68
Cdd:pfam01979 8 DAHVHLEMGLLRGIPVPpefayeALRLGITTMLksgtttvlDMGATTSTGIEA-LLEAAEElplglRFLGPGCsldTDGE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 69 FEPLMTLFLTNQTTPQDIIDAKQAGVTAcKLYPAGATTNSDAAVKGIQALypvfqAMqEQGLLLLIHgeVTEHHIDIFDR 148
Cdd:pfam01979 87 LEGRKALREKLKAGAEFIKGMADGVVFV-GLAPHGAPTFSDDELKAALEE-----AK-KYGLPVAIH--ALETKGEVEDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 149 EKVFIDTHL-------GPIVDAFPKLKVVFEHITTADAASfvagasefvgATITPQHLLLNRNDLlvggvrphnYCLPVL 221
Cdd:pfam01979 158 IAAFGGGIEhgthlevAESGGLLDIIKLILAHGVHLSPTE----------ANLLAEHLKGAGVAH---------CPFSNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 222 KRNTHQKALRDMVASGnKKFFLGTDSAPHarhkkeNACGCAGCYSAWsAIELYAEVFEQLGAIDKLEgFASHYGADFYGL 301
Cdd:pfam01979 219 KLRSGRIALRKALEDG-VKVGLGTDGAGS------GNSLNMLEELRL-ALELQFDPEGGLSPLEALR-MATINPAKALGL 289
|
...
gi 1832801142 302 PRN 304
Cdd:pfam01979 290 DDK 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
1-343 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 700.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 1 MQTLTITTPDDWHLHFRDNEMLAETVPATARCFQRAIVMPNLVPPVVNAEMAMAYKGRIEAARPKGSSFEPLMTLFLTNQ 80
Cdd:COG0418 2 MQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 81 TTPQDIIDAKQAG-VTACKLYPAGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEVTEHHIDIFDREKVFIDTHLGP 159
Cdd:COG0418 82 TTPEEIARAKASGvVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 160 IVDAFPKLKVVFEHITTADAASFVAGASEFVGATITPQHLLLNRNDLLVGGVRPHNYCLPVLKRNTHQKALRDMVASGNK 239
Cdd:COG0418 162 LRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 240 KFFLGTDSAPHARHKKENACGCAGCYSAWSAIELYAEVFEQLGAIDKLEGFASHYGADFYGLPRNTTTMTLVKESWTVPE 319
Cdd:COG0418 242 KFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPE 321
|
330 340
....*....|....*....|....
gi 1832801142 320 QVTLADGTdMVPFYAGQTLQWKLE 343
Cdd:COG0418 322 SIPFGDDT-LVPFRAGETLNWRVV 344
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
1-344 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 543.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 1 MQTLTITTPDDWHLHFRDNEMLAETVPATARCFQRAIVMPNLVPPVVNAEMAMAYKGRIEAARPKGSSFEPLMTLFLTNQ 80
Cdd:PLN02599 20 GTELTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 81 TTPQDIIDAKQAG-VTACKLYPAGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEVTEHHIDIFDREKVFIDTHLGP 159
Cdd:PLN02599 100 TTPEEIKAAKASGvVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 160 IVDAFPKLKVVFEHITTADAASFVAGASEF-VGATITPQHLLLNRNDLLVGGVRPHNYCLPVLKRNTHQKALRDMVASGN 238
Cdd:PLN02599 180 LVQKLPQLKIVMEHITTMDAVEFVESCGDGnVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 239 KKFFLGTDSAPHARHKKENACGCAGCYSAWSAIELYAEVFEQLGAIDKLEGFASHYGADFYGLPRNTTTMTLVKESWTVP 318
Cdd:PLN02599 260 KKFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVP 339
|
330 340
....*....|....*....|....*.
gi 1832801142 319 EQVTLADGTdMVPFYAGQTLQWKLEK 344
Cdd:PLN02599 340 EAYSFGGGT-VVPMFAGETIPWSVVS 364
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
4-340 |
5.27e-179 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 499.12 E-value: 5.27e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 4 LTITTPDDWHLHFRDNEMLAETVPATARCFQRAIVMPNLVPPVVNAEMAMAYKGRIEAARPkGSSFEPLMTLFLTNQTTP 83
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADP-GPNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 84 QDIIDAKQA-GVTACKLYPAGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEVTEHHIDIFDREKVFIdTHLGPIVD 162
Cdd:cd01294 80 EELREAKKKgGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 163 AFPKLKVVFEHITTADAASFVAGASEFVGATITPQHLLLNRNDLLVGGVRPHNYCLPVLKRNTHQKALRDMVASGNKKFF 242
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 243 LGTDSAPHARHKKENACGCAGCYSAWSAIELYAEVFEQLGAIDKLEGFASHYGADFYGLPRNTTTMTLVKESWTVPEQVT 322
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIP 318
|
330
....*....|....*...
gi 1832801142 323 LADGtDMVPFYAGQTLQW 340
Cdd:cd01294 319 FGNN-GVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
4-342 |
1.62e-158 |
|
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in microbial genomes than a related dihydroorotase that appears in a complex with aspartyltranscarbamoylase or as a homologous domain in multifunctional proteins of pyrimidine biosynthesis in higher eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 129935 Cd Length: 341 Bit Score: 447.34 E-value: 1.62e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 4 LTITTPDDWHLHFRDNEMLAETVPATARCFQRAIVMPNLVPPVVNAEMAMAYKGRIEAARPKGSSFEPLMTLFLTNQTTP 83
Cdd:TIGR00856 2 LTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 84 QDIIDAK-QAGVTACKLYPAGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEVTEHHIDIFDREKVFIDTHLGPIVD 162
Cdd:TIGR00856 82 EELERAKnEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 163 AFPKLKVVFEHITTADAASFVAGASEFVGATITPQHLLLNRNDLLVGGVRPHNYCLPVLKRNTHQKALRDMVASGNKKFF 242
Cdd:TIGR00856 162 RFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKFF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 243 LGTDSAPHARHKKENACGCAGCYSAWSAIELYAEVFEQLGAIDKLEGFASHYGADFYGLPRNTTTMTLVKESWTVPEQVT 322
Cdd:TIGR00856 242 LGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESIA 321
|
330 340
....*....|....*....|
gi 1832801142 323 LADGTdMVPFYAGQTLQWKL 342
Cdd:TIGR00856 322 LTDDT-LVPFRAGETLSWSV 340
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
11-256 |
7.67e-12 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 65.43 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 11 DWHLHFRDNEM------LAETVPATARCFQRAIVMPNLVPPVVNAEmamAYKGRIEAARpKGSSFEPLMTLFLTNQTTPQ 84
Cdd:cd01318 10 DIHVHFREPGLtykedfVSGSRAAAAGGVTTVMDMPNTKPPTTTAE---ALYEKLRLAA-AKSVVDYGLYFGVTGSEDLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 85 DIIDAKQAGVtacKLYPAGATtnsdaavKGIQALYPVFQAMQEQG-LLLLIHGEVTEHhidIFDREKVFIDTHLGP-IVD 162
Cdd:cd01318 86 ELDKAPPAGY---KIFMGDST-------GDLLDDEETLERIFAEGsVLVTFHAEDEDR---LRENRKELKGESAHPrIRD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 163 AFP---------------KLKVVFEHITTADAASFVAGASEFVGATITPQHLLLNRNDLLVGGVRPHnyCLPVLKRNTHQ 227
Cdd:cd01318 153 AEAaavataralklarrhGARLHICHVSTPEELKLIKKAKPGVTVEVTPHHLFLDVEDYDRLGTLGK--VNPPLRSREDR 230
|
250 260
....*....|....*....|....*....
gi 1832801142 228 KALRDMVASGnKKFFLGTDSAPHARHKKE 256
Cdd:cd01318 231 KALLQALADG-RIDVIASDHAPHTLEEKR 258
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
11-304 |
1.64e-10 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 61.36 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 11 DWHLHFRDNEMLAETVP------ATARCFQRAI--------VMPNLVPPVVNAeMAMAYKG-----RIEAARP---KGSS 68
Cdd:pfam01979 8 DAHVHLEMGLLRGIPVPpefayeALRLGITTMLksgtttvlDMGATTSTGIEA-LLEAAEElplglRFLGPGCsldTDGE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 69 FEPLMTLFLTNQTTPQDIIDAKQAGVTAcKLYPAGATTNSDAAVKGIQALypvfqAMqEQGLLLLIHgeVTEHHIDIFDR 148
Cdd:pfam01979 87 LEGRKALREKLKAGAEFIKGMADGVVFV-GLAPHGAPTFSDDELKAALEE-----AK-KYGLPVAIH--ALETKGEVEDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 149 EKVFIDTHL-------GPIVDAFPKLKVVFEHITTADAASfvagasefvgATITPQHLLLNRNDLlvggvrphnYCLPVL 221
Cdd:pfam01979 158 IAAFGGGIEhgthlevAESGGLLDIIKLILAHGVHLSPTE----------ANLLAEHLKGAGVAH---------CPFSNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 222 KRNTHQKALRDMVASGnKKFFLGTDSAPHarhkkeNACGCAGCYSAWsAIELYAEVFEQLGAIDKLEgFASHYGADFYGL 301
Cdd:pfam01979 219 KLRSGRIALRKALEDG-VKVGLGTDGAGS------GNSLNMLEELRL-ALELQFDPEGGLSPLEALR-MATINPAKALGL 289
|
...
gi 1832801142 302 PRN 304
Cdd:pfam01979 290 DDK 292
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
37-303 |
1.25e-09 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 58.95 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 37 IVMPNLVPPVVNAEmAMAYKgrIEAARPKGSS-FEPLMTLFLTNQTTPQDIIDAKQAGVTACKLYPAGATTN--SDAAVk 113
Cdd:COG0044 86 VDMPNTNPVTDTPE-ALEFK--LARAEEKALVdVGPHGALTKGLGENLAELGALAEAGAVAFKVFMGSDDGNpvLDDGL- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 114 giqaLYPVFQAMQEQGLLLLIH--------------GEV-TEHHIDIFDREK----VFIDTHLGPIVDAfpKLKVVfeHI 174
Cdd:COG0044 162 ----LRRALEYAAEFGALVAVHaedpdlirggvmneGKTsPRLGLKGRPAEAeeeaVARDIALAEETGA--RLHIV--HV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 175 TTADAASFVAGASEfVGATIT----PQHLLLNRNDLLVGGVRPHnyCLPVLKRNTHQKALRDMVASGNkkF-FLGTDSAP 249
Cdd:COG0044 234 STAEAVELIREAKA-RGLPVTaevcPHHLTLTDEDLERYGTNFK--VNPPLRTEEDREALWEGLADGT--IdVIATDHAP 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832801142 250 HARHKKEN-----ACGCAGCYSAWSAieLYAEVFEQlGAIDkLEGFA---SHYGADFYGLPR 303
Cdd:COG0044 309 HTLEEKELpfaeaPNGIPGLETALPL--LLTELVHK-GRLS-LERLVellSTNPARIFGLPR 366
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
11-255 |
2.87e-09 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 57.84 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 11 DWHLHFRD-NEMLAETV-----PATARCFQRAIVMPNLVPPVVNAEMAMAYKGRIEaarpKGSSFEPLMTLFLTNQTTPQ 84
Cdd:TIGR00857 43 DLHVHLRDpGEEYKEDIesgskAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLK----KVSLVDVHLYGGVTQGNQGK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 85 DIIDA---KQAGVTacklypAGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEvtehHIDIFDREKVFIDT-----H 156
Cdd:TIGR00857 119 ELTEAyelKEAGAV------GRMFTDDGSEVQDILSMRRALEYAAIAGVPIALHAE----DPDLIYGGVMHEGPsaaqlG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 157 LGPI------------VDAFPKL--KVVFEHITTADAASFVAGASEF---VGATITPQHLLLNRNDllVGGVRPHNYCLP 219
Cdd:TIGR00857 189 LPARppeaeevavarlLELAKHAgcPVHICHISTKESLELIVKAKSQgikITAEVTPHHLLLSEED--VARLDGNGKVNP 266
|
250 260 270
....*....|....*....|....*....|....*.
gi 1832801142 220 VLKRNTHQKALRDMVASGNKKFFlGTDSAPHARHKK 255
Cdd:TIGR00857 267 PLREKEDRLALIEGLKDGIIDII-ATDHAPHTLEEK 301
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
168-258 |
5.47e-07 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 50.70 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 168 KVVFEHITTADAASFVAGASEF---VGATITPQHLLLnrNDLLVGGVRPHNYCLPVLKRNTHQKALRDMVASGnKKFFLG 244
Cdd:cd01317 187 RVHFQHLSTARSLELIRKAKAKglpVTAEVTPHHLLL--DDEALESYDTNAKVNPPLRSEEDREALIEALKDG-TIDAIA 263
|
90
....*....|....
gi 1832801142 245 TDSAPHARHKKENA 258
Cdd:cd01317 264 SDHAPHTDEEKDLP 277
|
|
| LigW |
COG2159 |
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ... |
11-173 |
8.22e-07 |
|
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];
Pssm-ID: 441762 [Multi-domain] Cd Length: 253 Bit Score: 49.59 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 11 DWHLHFRDNEMLAETVpaTARCFQRAIVMPNLVPPVVNAEMAMAYKGRI-EAARPKGSSFEPLMTLFltnqttPQDIIDA 89
Cdd:COG2159 5 DVHTHLGTPEERLADM--DEAGIDKAVLSPTPLADPELAALARAANDWLaELVARYPDRFIGFATVD------PQDPDAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 90 --------KQAGVTACKLYPAGATTNSDAAvkgiqALYPVFQAMQEQGLLLLIHGEVTEHHIDIFDREkVFIDTHLGPIV 161
Cdd:COG2159 77 veeleravEELGFRGVKLHPAVGGFPLDDP-----RLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLY-YAAPLILSGVA 150
|
170
....*....|..
gi 1832801142 162 DAFPKLKVVFEH 173
Cdd:COG2159 151 ERFPDLKFILAH 162
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
11-258 |
1.59e-05 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 46.23 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 11 DWHLHFRD-------NEMLAETVPATARCFQRAIVMPNLVPPVVNA-EMAMAYKGRIEAARpkgSSFeplmTLFL---TN 79
Cdd:cd01302 9 DIHVHLRDpggttykEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLpAIELKIKLAEESSY---VDF----SFHAgigPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 80 QTTPQdIIDAKQAGVTACKLYpaGATTNSDAAVKGIQALYPVFQAMQEQGLLLLIHGEvtehhidifdrekvfidtHLGP 159
Cdd:cd01302 82 DVTDE-LKKLFDAGINSLKVF--MNYYFGELFDVDDGTLMRTFLEIASRGGPVMVHAE------------------RAAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 160 IVDAFpKLKVVFEHITTADAASFVAGASEF---VGATITPQHLLLNRNDLLVGG----VRPhnyclPVLKRNtHQKALRD 232
Cdd:cd01302 141 LAEEA-GANVHIAHVSSGEALELIKFAKNKgvkVTCEVCPHHLFLDESMLRLNGawgkVNP-----PLRSKE-DREALWE 213
|
250 260
....*....|....*....|....*.
gi 1832801142 233 MVASGnKKFFLGTDSAPHARHKKENA 258
Cdd:cd01302 214 GVKNG-KIDTIASDHAPHSKEEKESG 238
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
11-251 |
7.04e-05 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 43.86 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 11 DWHLHFRDNEM-----------LAETVPATARCFQR-------------AIVMPNLVPPV----VNAEMAMAYKG--RIE 60
Cdd:cd01292 3 DTHVHLDGSALrgtrlnlelkeAEELSPEDLYEDTLraleallaggvttVVDMGSTPPPTttkaAIEAVAEAARAsaGIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 61 AARPKGSSFEPLMTLFLTNQTTPQDIIDAKQAGVTACKLYPAGATTNSDAAVkgiqaLYPVFQAMQEQGLLLLIHGEVTE 140
Cdd:cd01292 83 VVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDES-----LRRVLEEARKLGLPVVIHAGELP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 141 HHIDIFDRekvFIDTHLGPivdafpkLKVVFEHITTADAASFVAGASEFVGATITPQHLLLNRNDllvggvrphnyclpv 220
Cdd:cd01292 158 DPTRALED---LVALLRLG-------GRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRD--------------- 212
|
250 260 270
....*....|....*....|....*....|.
gi 1832801142 221 lkrNTHQKALRDMVASGNkKFFLGTDSAPHA 251
Cdd:cd01292 213 ---GEGAEALRRLLELGI-RVTLGTDGPPHP 239
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
11-263 |
9.88e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 43.99 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 11 DWHLHFRD-NEMLAETVPA-TARCFQRAIV----MPNLVPPVVNAEMamaYKGRIEAARpkGSSFEPLMTLFLTNQttpq 84
Cdd:PRK04250 51 DVHVHLRDfEESYKETIESgTKAALHGGITlvfdMPNTKPPIMDEKT---YEKRMRIAE--KKSYADYALNFLIAG---- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 85 diiDAKQAGVTACKLYPAGATtnsdAAVKGIqaLYPVFQAMQEQGL-LLLIHGEVTEHHIDIFDREKVFIDTHLGPIVDA 163
Cdd:PRK04250 122 ---NCEKAEEIKADFYKIFMG----ASTGGI--FSENFEVDYACAPgIVSVHAEDPELIREFPERPPEAEVVAIERALEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 164 FPKLKVVFE--HITTADAASFVAGAS-EFVGATITPQHLLLNRNDLLVGGVRPHNyclPVLKRNTHQKALrdmVASGNKK 240
Cdd:PRK04250 193 GKKLKKPLHicHISTKDGLKLILKSNlPWVSFEVTPHHLFLTRKDYERNPLLKVY---PPLRSEEDRKAL---WENFSKI 266
|
250 260
....*....|....*....|...
gi 1832801142 241 FFLGTDSAPHARHKKENacGCAG 263
Cdd:PRK04250 267 PIIASDHAPHTLEDKEA--GAAG 287
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
173-256 |
2.73e-04 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 42.49 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 173 HITTADAASFVAGASEF---VGATITPQHLLLNRNDLLvgGVRPHNYCLPVLKRNTHQKALRDMVASGNKKFfLGTDSAP 249
Cdd:PRK09357 231 HVSTAGSVELIRWAKALgikVTAEVTPHHLLLTDEDLL--TYDPNYKVNPPLRTEEDREALIEGLKDGTIDA-IATDHAP 307
|
....*..
gi 1832801142 250 HARHKKE 256
Cdd:PRK09357 308 HAREEKE 314
|
|
| Amidohydro_2 |
pfam04909 |
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979. |
81-173 |
7.91e-04 |
|
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
Pssm-ID: 428190 [Multi-domain] Cd Length: 283 Bit Score: 40.59 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 81 TTPQDIIDAKQAGVTACKLYPAGattnSDAAVKGIQALYPVFQAMQEQGLLLLIHGEVTEHHIDIFdrekVFIDTHLGPI 160
Cdd:pfam04909 91 AAAELERAVGEAGFRGVRLNPHP----GGDPLLGDRLDRPIYEALEELGLPVDIHTGFGDRPEDTR----AIQPLLLAGV 162
|
90
....*....|...
gi 1832801142 161 VDAFPKLKVVFEH 173
Cdd:pfam04909 163 ARKFPDLKIVLDH 175
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
171-256 |
9.12e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 40.79 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832801142 171 FEHITTADAASFVAGAsefvGAT--ITPQHLLLNRNDLlvGGVRPHNYCLPVLKRNTHQKALRDMVASGNKKfFLGTDSA 248
Cdd:PRK02382 232 IAHISTPEGVDAARRE----GITceVTPHHLFLSRRDW--ERLGTFGKMNPPLRSEKRREALWERLNDGTID-VVASDHA 304
|
....*...
gi 1832801142 249 PHARHKKE 256
Cdd:PRK02382 305 PHTREEKD 312
|
|
| |
