|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
1-342 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 705.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 1 MTQLTITRPDDWHVHLRDGEVLKDTVRDISRYNGRALIMPNTIPPVTDTEMALAYRERIMAEQPSE-QFQPLMALYLTDN 79
Cdd:COG0418 2 MQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGsDFEPLMTLYLTDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 80 TTPDEIRKAKESGAVVAAKLYPAGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEVTAHDVDIFDREKEFLDTVLAP 159
Cdd:COG0418 82 TTPEEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 160 IVNDFPNLKIVLEHITTADAATFVKNANENVAATITAHHLLYNRNHMLVGGIKPHFYCLPILKRNTHQLALIEAATSGSK 239
Cdd:COG0418 162 LRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 240 KFFLGTDSAPHAKGAKESACGCAGSYTAHAAVELYAEVFDLEGKIENLEAFASHNGPDFYGMPRNADTITLVKEEWNVAE 319
Cdd:COG0418 242 KFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPE 321
|
330 340
....*....|....*....|...
gi 497531564 320 TMPFGSDIVVPIRGGETIAWSVK 342
Cdd:COG0418 322 SIPFGDDTLVPFRAGETLNWRVV 344
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
1-341 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 573.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 1 MTQLTITRPDDWHVHLRDGEVLKDTVRDISRYNGRALIMPNTIPPVTDTEMALAYRERIMAEQPSE-QFQPLMALYLTDN 79
Cdd:PLN02599 20 GTELTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGsSFEPLMTLYLTDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 80 TTPDEIRKAKESGAVVAAKLYPAGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEVTAHDVDIFDREKEFLDTVLAP 159
Cdd:PLN02599 100 TTPEEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 160 IVNDFPNLKIVLEHITTADAATFVKNANE-NVAATITAHHLLYNRNHMLVGGIKPHFYCLPILKRNTHQLALIEAATSGS 238
Cdd:PLN02599 180 LVQKLPQLKIVMEHITTMDAVEFVESCGDgNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 239 KKFFLGTDSAPHAKGAKESACGCAGSYTAHAAVELYAEVFDLEGKIENLEAFASHNGPDFYGMPRNADTITLVKEEWNVA 318
Cdd:PLN02599 260 KKFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVP 339
|
330 340
....*....|....*....|...
gi 497531564 319 ETMPFGSDIVVPIRGGETIAWSV 341
Cdd:PLN02599 340 EAYSFGGGTVVPMFAGETIPWSV 362
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
4-339 |
0e+00 |
|
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: 534.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 4 LTITRPDDWHVHLRDGEVLKDTVRDISRYNGRALIMPNTIPPVTDTEMALAYRERIMAEQPSEQFQPLMALYLTDNTTPD 83
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADPGPNFTPLMTLYLTENTTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 84 EIRKAKESGAVVAAKLYPAGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEVTAHDVDIFDREKEFLdTVLAPIVND 163
Cdd:cd01294 81 ELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 164 FPNLKIVLEHITTADAATFVKNANENVAATITAHHLLYNRNHMLVGGIKPHFYCLPILKRNTHQLALIEAATSGSKKFFL 243
Cdd:cd01294 160 FPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFFL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 244 GTDSAPHAKGAKESACGCAGSYTAHAAVELYAEVFDLEGKIENLEAFASHNGPDFYGMPRNADTITLVKEEWNVAETMPF 323
Cdd:cd01294 240 GSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIPF 319
|
330
....*....|....*.
gi 497531564 324 GSDIVVPIRGGETIAW 339
Cdd:cd01294 320 GNNGVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
3-342 |
5.27e-167 |
|
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: 468.53 E-value: 5.27e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 3 QLTITRPDDWHVHLRDGEVLKDTVRDISRYNGRALIMPNTIPPVTDTEMALAYRERIMAEQPS-EQFQPLMALYLTDNTT 81
Cdd:TIGR00856 1 ELTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAgHDFTPLMTLYLTDSLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 82 PDEIRKAKESGAVVAAKLYPAGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEVTAHDVDIFDREKEFLDTVLAPIV 161
Cdd:TIGR00856 81 PEELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 162 NDFPNLKIVLEHITTADAATFVKNANENVAATITAHHLLYNRNHMLVGGIKPHFYCLPILKRNTHQLALIEAATSGSKKF 241
Cdd:TIGR00856 161 QRFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 242 FLGTDSAPHAKGAKESACGCAGSYTAHAAVELYAEVFDLEGKIENLEAFASHNGPDFYGMPRNADTITLVKEEWNVAETM 321
Cdd:TIGR00856 241 FLGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESI 320
|
330 340
....*....|....*....|.
gi 497531564 322 PFGSDIVVPIRGGETIAWSVK 342
Cdd:TIGR00856 321 ALTDDTLVPFRAGETLSWSVK 341
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
11-309 |
1.56e-08 |
|
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: 55.20 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRDGEVLKDTVR-DISRYNGRALIMPNTIPPVT---DTEMALAYRERIMAEQPSEQFQ--------PLMALYLTD 78
Cdd:pfam01979 8 DAHVHLEMGLLRGIPVPpEFAYEALRLGITTMLKSGTTtvlDMGATTSTGIEALLEAAEELPLglrflgpgCSLDTDGEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 79 NTTPDEIRKAKE--------SGAVVAAKLYPAGATTNSDSGvtsaqkIYHVLEAMQEVGMLLLVHgeVTAHDVDIFDREK 150
Cdd:pfam01979 88 EGRKALREKLKAgaefikgmADGVVFVGLAPHGAPTFSDDE------LKAALEEAKKYGLPVAIH--ALETKGEVEDAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 151 EFLDTVL-------APIVNDFPNLKIVLEHITTADAATfvknanenvaATITAHHLlynRNHMLVggikphFYCLPILKR 223
Cdd:pfam01979 160 AFGGGIEhgthlevAESGGLLDIIKLILAHGVHLSPTE----------ANLLAEHL---KGAGVA------HCPFSNSKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 224 NTHQLALIEAATSGsKKFFLGTDSAPHAKgakesaCGCAGSYTAHAAvelyAEVFDLEGKIENLEAF--ASHNGPDFYGM 301
Cdd:pfam01979 221 RSGRIALRKALEDG-VKVGLGTDGAGSGN------SLNMLEELRLAL----ELQFDPEGGLSPLEALrmATINPAKALGL 289
|
....*...
gi 497531564 302 PRNADTIT 309
Cdd:pfam01979 290 DDKVGSIE 297
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
1-342 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 705.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 1 MTQLTITRPDDWHVHLRDGEVLKDTVRDISRYNGRALIMPNTIPPVTDTEMALAYRERIMAEQPSE-QFQPLMALYLTDN 79
Cdd:COG0418 2 MQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGsDFEPLMTLYLTDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 80 TTPDEIRKAKESGAVVAAKLYPAGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEVTAHDVDIFDREKEFLDTVLAP 159
Cdd:COG0418 82 TTPEEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 160 IVNDFPNLKIVLEHITTADAATFVKNANENVAATITAHHLLYNRNHMLVGGIKPHFYCLPILKRNTHQLALIEAATSGSK 239
Cdd:COG0418 162 LRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 240 KFFLGTDSAPHAKGAKESACGCAGSYTAHAAVELYAEVFDLEGKIENLEAFASHNGPDFYGMPRNADTITLVKEEWNVAE 319
Cdd:COG0418 242 KFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPE 321
|
330 340
....*....|....*....|...
gi 497531564 320 TMPFGSDIVVPIRGGETIAWSVK 342
Cdd:COG0418 322 SIPFGDDTLVPFRAGETLNWRVV 344
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
1-341 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 573.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 1 MTQLTITRPDDWHVHLRDGEVLKDTVRDISRYNGRALIMPNTIPPVTDTEMALAYRERIMAEQPSE-QFQPLMALYLTDN 79
Cdd:PLN02599 20 GTELTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGsSFEPLMTLYLTDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 80 TTPDEIRKAKESGAVVAAKLYPAGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEVTAHDVDIFDREKEFLDTVLAP 159
Cdd:PLN02599 100 TTPEEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 160 IVNDFPNLKIVLEHITTADAATFVKNANE-NVAATITAHHLLYNRNHMLVGGIKPHFYCLPILKRNTHQLALIEAATSGS 238
Cdd:PLN02599 180 LVQKLPQLKIVMEHITTMDAVEFVESCGDgNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 239 KKFFLGTDSAPHAKGAKESACGCAGSYTAHAAVELYAEVFDLEGKIENLEAFASHNGPDFYGMPRNADTITLVKEEWNVA 318
Cdd:PLN02599 260 KKFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVP 339
|
330 340
....*....|....*....|...
gi 497531564 319 ETMPFGSDIVVPIRGGETIAWSV 341
Cdd:PLN02599 340 EAYSFGGGTVVPMFAGETIPWSV 362
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
4-339 |
0e+00 |
|
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: 534.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 4 LTITRPDDWHVHLRDGEVLKDTVRDISRYNGRALIMPNTIPPVTDTEMALAYRERIMAEQPSEQFQPLMALYLTDNTTPD 83
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADPGPNFTPLMTLYLTENTTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 84 EIRKAKESGAVVAAKLYPAGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEVTAHDVDIFDREKEFLdTVLAPIVND 163
Cdd:cd01294 81 ELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 164 FPNLKIVLEHITTADAATFVKNANENVAATITAHHLLYNRNHMLVGGIKPHFYCLPILKRNTHQLALIEAATSGSKKFFL 243
Cdd:cd01294 160 FPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFFL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 244 GTDSAPHAKGAKESACGCAGSYTAHAAVELYAEVFDLEGKIENLEAFASHNGPDFYGMPRNADTITLVKEEWNVAETMPF 323
Cdd:cd01294 240 GSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIPF 319
|
330
....*....|....*.
gi 497531564 324 GSDIVVPIRGGETIAW 339
Cdd:cd01294 320 GNNGVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
3-342 |
5.27e-167 |
|
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: 468.53 E-value: 5.27e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 3 QLTITRPDDWHVHLRDGEVLKDTVRDISRYNGRALIMPNTIPPVTDTEMALAYRERIMAEQPS-EQFQPLMALYLTDNTT 81
Cdd:TIGR00856 1 ELTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAgHDFTPLMTLYLTDSLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 82 PDEIRKAKESGAVVAAKLYPAGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEVTAHDVDIFDREKEFLDTVLAPIV 161
Cdd:TIGR00856 81 PEELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 162 NDFPNLKIVLEHITTADAATFVKNANENVAATITAHHLLYNRNHMLVGGIKPHFYCLPILKRNTHQLALIEAATSGSKKF 241
Cdd:TIGR00856 161 QRFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 242 FLGTDSAPHAKGAKESACGCAGSYTAHAAVELYAEVFDLEGKIENLEAFASHNGPDFYGMPRNADTITLVKEEWNVAETM 321
Cdd:TIGR00856 241 FLGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESI 320
|
330 340
....*....|....*....|.
gi 497531564 322 PFGSDIVVPIRGGETIAWSVK 342
Cdd:TIGR00856 321 ALTDDTLVPFRAGETLSWSVK 341
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
11-342 |
2.77e-16 |
|
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: 78.92 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRD-GEVLKDTVRDISR---YNGRALI--MPNTIPPVTDTEmALAYRERIMAEQPSEQFqplmALY--LTDNTTP 82
Cdd:cd01318 10 DIHVHFREpGLTYKEDFVSGSRaaaAGGVTTVmdMPNTKPPTTTAE-ALYEKLRLAAAKSVVDY----GLYfgVTGSEDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 83 DEIRKAKesgaVVAAKLYPaGATTNSDsgvtsaQKIYHVLE-AMQEVGMLLLVHGEvtahDVDIFD-REKEFLDTVLAPI 160
Cdd:cd01318 85 EELDKAP----PAGYKIFM-GDSTGDL------LDDEETLErIFAEGSVLVTFHAE----DEDRLReNRKELKGESAHPR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 161 VND----------------FPNLKIVLEHITTADAATFVKNANENVAATITAHHLLYNRNHmlVGGIKPHFYCLPILKRN 224
Cdd:cd01318 150 IRDaeaaavataralklarRHGARLHICHVSTPEELKLIKKAKPGVTVEVTPHHLFLDVED--YDRLGTLGKVNPPLRSR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 225 THQLALIEAATSGSKKfFLGTDSAPH-----AKGAKESACGCAGSYTAHAAVELYAEVFDLEgkIENLEAFASHNGPDFY 299
Cdd:cd01318 228 EDRKALLQALADGRID-VIASDHAPHtleekRKGYPAAPSGIPGVETALPLMLTLVNKGILS--LSRVVRLTSHNPARIF 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 497531564 300 GMPRN--------ADtITLV--KEEWNVAeTMPFGS-DIVVPIRGGETIAWSVK 342
Cdd:cd01318 305 GIKNKgriaegydAD-LTVVdlKEERTIR-AEEFHSkAGWTPFEGFEVTGFPVM 356
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
11-251 |
4.76e-14 |
|
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: 72.48 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRD-GEVLKDTVRDISRYNGR-----ALIMPNTIPPVTDTEmalAYRERIMAEQPSEQFQPLMALYLTDNTTPDE 84
Cdd:TIGR00857 43 DLHVHLRDpGEEYKEDIESGSKAAAHggfttVADMPNTKPPIDTPE---TLEWKLQRLKKVSLVDVHLYGGVTQGNQGKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 85 IRKAKESGAVVAAklypAGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEvtahDVDIFDREKEFLDTVLA------ 158
Cdd:TIGR00857 120 LTEAYELKEAGAV----GRMFTDDGSEVQDILSMRRALEYAAIAGVPIALHAE----DPDLIYGGVMHEGPSAAqlglpa 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 159 -PIVNDFPNLKIVLE------------HITTADAATFVKNANE---NVAATITAHHLLYNRNHmlVGGIKPHFYCLPILK 222
Cdd:TIGR00857 192 rPPEAEEVAVARLLElakhagcpvhicHISTKESLELIVKAKSqgiKITAEVTPHHLLLSEED--VARLDGNGKVNPPLR 269
|
250 260
....*....|....*....|....*....
gi 497531564 223 RNTHQLALIEAATSGSKKFFlGTDSAPHA 251
Cdd:TIGR00857 270 EKEDRLALIEGLKDGIIDII-ATDHAPHT 297
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
11-256 |
2.26e-09 |
|
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: 58.02 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRD-GEVLKDTVRDISR------YnGRALIMPNTIPPVTDTEMALAYRERIMAEQPSEQFqPLMALyltdntTPD 83
Cdd:cd01317 18 DLHVHLREpGFEYKETLESGAKaaaaggF-TTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRVL-PIGAL------TKG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 84 -------EIRKAKESGAVvaaklypagATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEvtahDVDIFD----REKEF 152
Cdd:cd01317 90 lkgeeltEIGELLEAGAV---------GFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPE----DPSLAGggvmNEGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 153 -----------------LDTVLApIVNDFPNlKIVLEHITTADAATFVKNANE---NVAATITAHHLLYNRNhmLVGGIK 212
Cdd:cd01317 157 asrlglpgippeaetimVARDLE-LAEATGA-RVHFQHLSTARSLELIRKAKAkglPVTAEVTPHHLLLDDE--ALESYD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 497531564 213 PHFYCLPILKRNTHQLALIEAATSGSKKfFLGTDSAPHAKGAKE 256
Cdd:cd01317 233 TNAKVNPPLRSEEDREALIEALKDGTID-AIASDHAPHTDEEKD 275
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
11-317 |
2.76e-09 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 57.86 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRD-GEVLKDTVRDISR---YNGRALI--MPNTIPPVTDTEMaLAYRERIMAEQPSEQFqplmALYLTDNTTPDE 84
Cdd:PRK04250 51 DVHVHLRDfEESYKETIESGTKaalHGGITLVfdMPNTKPPIMDEKT-YEKRMRIAEKKSYADY----ALNFLIAGNCEK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 85 IRKAKesgavvaAKLYPAGAttnsdsgVTSAQKIYhvLEAMQE----VGMLLLVHGEvtahDVDIFDREKEflDTVLAPI 160
Cdd:PRK04250 126 AEEIK-------ADFYKIFM-------GASTGGIF--SENFEVdyacAPGIVSVHAE----DPELIREFPE--RPPEAEV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 161 VNDFPNLKIVLE--------HITTADAATFVKNAN-ENVAATITAHHLLYNRNHMLVGgikPHFYCLPILKRNTHQLALI 231
Cdd:PRK04250 184 VAIERALEAGKKlkkplhicHISTKDGLKLILKSNlPWVSFEVTPHHLFLTRKDYERN---PLLKVYPPLRSEEDRKALW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 232 EaatSGSKKFFLGTDSAPHAKGAKES-ACGCAGSYTAH-----AAVELYAEVFDLEGKI-ENLEAFASHNGPDFyGMPRN 304
Cdd:PRK04250 261 E---NFSKIPIIASDHAPHTLEDKEAgAAGIPGLETEVpllldAANKGMISLFDIVEKMhDNPARIFGIKNYGI-EEGNY 336
|
330
....*....|....
gi 497531564 305 AD-TITLVKEEWNV 317
Cdd:PRK04250 337 ANfAVFDMKKEWTI 350
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
11-258 |
6.23e-09 |
|
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: 56.63 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRDGE--VLKDTVRDISR---YNGRALI--MPNTIPPVTDTemaLAYRERIMAEQPSEQFQPLMALYLTDNTTPD 83
Cdd:cd01302 9 DIHVHLRDPGgtTYKEDFESGSRaaaAGGVTTVidMPNTGPPPIDL---PAIELKIKLAEESSYVDFSFHAGIGPGDVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 84 EIRKAKESGaVVAAKLYpaGATTNSDSGVTSAQKIYHVLEAMQEVGMLLLVHGEVTAHdvdifdREKEFldtvlapivnd 163
Cdd:cd01302 86 ELKKLFDAG-INSLKVF--MNYYFGELFDVDDGTLMRTFLEIASRGGPVMVHAERAAQ------LAEEA----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 164 fpNLKIVLEHITTADA---ATFVKNANENVAATITAHHLLYNRNHMLVGGIKphFYCLPILKRNTHQLALIEAATSGsKK 240
Cdd:cd01302 146 --GANVHIAHVSSGEAlelIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAW--GKVNPPLRSKEDREALWEGVKNG-KI 220
|
250
....*....|....*...
gi 497531564 241 FFLGTDSAPHAKGAKESA 258
Cdd:cd01302 221 DTIASDHAPHSKEEKESG 238
|
|
| LigW |
COG2159 |
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ... |
11-173 |
1.00e-08 |
|
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];
Pssm-ID: 441762 [Multi-domain] Cd Length: 253 Bit Score: 55.37 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRDGEvlkDTVRDISRYN-GRALIMPNTIPPVTDTEMALAYRERI--MAEQPSEQFQPLMALYLTD-NTTPDEIR 86
Cdd:COG2159 5 DVHTHLGTPE---ERLADMDEAGiDKAVLSPTPLADPELAALARAANDWLaeLVARYPDRFIGFATVDPQDpDAAVEELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 87 KAKESGAVVAAKLYPAGATTNSDSgvtsaQKIYHVLEAMQEVGMLLLVHGEVTAHDVDIFDREkEFLDTVLAPIVNDFPN 166
Cdd:COG2159 82 RAVEELGFRGVKLHPAVGGFPLDD-----PRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLY-YAAPLILSGVAERFPD 155
|
....*..
gi 497531564 167 LKIVLEH 173
Cdd:COG2159 156 LKFILAH 162
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
11-309 |
1.56e-08 |
|
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: 55.20 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRDGEVLKDTVR-DISRYNGRALIMPNTIPPVT---DTEMALAYRERIMAEQPSEQFQ--------PLMALYLTD 78
Cdd:pfam01979 8 DAHVHLEMGLLRGIPVPpEFAYEALRLGITTMLKSGTTtvlDMGATTSTGIEALLEAAEELPLglrflgpgCSLDTDGEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 79 NTTPDEIRKAKE--------SGAVVAAKLYPAGATTNSDSGvtsaqkIYHVLEAMQEVGMLLLVHgeVTAHDVDIFDREK 150
Cdd:pfam01979 88 EGRKALREKLKAgaefikgmADGVVFVGLAPHGAPTFSDDE------LKAALEEAKKYGLPVAIH--ALETKGEVEDAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 151 EFLDTVL-------APIVNDFPNLKIVLEHITTADAATfvknanenvaATITAHHLlynRNHMLVggikphFYCLPILKR 223
Cdd:pfam01979 160 AFGGGIEhgthlevAESGGLLDIIKLILAHGVHLSPTE----------ANLLAEHL---KGAGVA------HCPFSNSKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 224 NTHQLALIEAATSGsKKFFLGTDSAPHAKgakesaCGCAGSYTAHAAvelyAEVFDLEGKIENLEAF--ASHNGPDFYGM 301
Cdd:pfam01979 221 RSGRIALRKALEDG-VKVGLGTDGAGSGN------SLNMLEELRLAL----ELQFDPEGGLSPLEALrmATINPAKALGL 289
|
....*...
gi 497531564 302 PRNADTIT 309
Cdd:pfam01979 290 DDKVGSIE 297
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
11-255 |
8.99e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 50.24 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRD-GEVLKD-----TVRDIsrYNGRALI--MPNTIPPVTDTEmALAYRERIMAEQPSEQFqplmALYLTDNTTP 82
Cdd:PRK01211 50 DIHVHFRTpGETEKEdfstgTLSAI--FGGTTFImdMPNNNIPIKDYN-AFSDKLGRVAPKAYVDF----SLYSMETGNN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 83 DEIRKAKESGavvaAKLYpAGATTNSDSGVTSAQKIyhvlEAMQEVGMLLLVHGEVTAHDVDIFDREKEFLDTVLA-PI- 160
Cdd:PRK01211 123 ALILDERSIG----LKVY-MGGTTNTNGTDIEGGEI----KKINEANIPVFFHAELSECLRKHQFESKNLRDHDLArPIe 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 161 -----VNDFPNLKI---VLEHITTADAATfvknaneNVAATITAHHLLYNRNHML--VGGIKPhfyclPILKRNTHQLaL 230
Cdd:PRK01211 194 ceikaVKYVKNLDLktkIIAHVSSIDVIG-------RFLREVTPHHLLLNDDMPLgsYGKVNP-----PLRDRWTQER-L 260
|
250 260
....*....|....*....|....*.
gi 497531564 231 IEAATSGskKF-FLGTDSAPHAKGAK 255
Cdd:PRK01211 261 LEEYISG--RFdILSSDHAPHTEEDK 284
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
11-319 |
2.36e-06 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 49.04 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 11 DWHVHLRD-GEVLKDTVRDISRyngrA---------LIMPNTIPpVTDTEMALAYRERIMAEQPSEQFQPLMALylTDNT 80
Cdd:PRK09357 57 DLHVHLREpGQEDKETIETGSR----AaaaggfttvVAMPNTKP-VIDTPEVVEYVLDRAKEAGLVDVLPVGAI--TKGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 81 TPDEIrkakesgaVVAAKLYPAGATTNSDSG--VTSAQKIYHVLEAMQEVGMLLLVHGEVT-------AHDVDIfdreKE 151
Cdd:PRK09357 130 AGEEL--------TEFGALKEAGVVAFSDDGipVQDARLMRRALEYAKALDLLIAQHCEDPslteggvMNEGEV----SA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 152 FLDTVLAPIVND----FPNLKIVLE--------HITTADAA---TFVKNANENVAATITAHHLLYNRNHMLvgGIKPHFY 216
Cdd:PRK09357 198 RLGLPGIPAVAEevmiARDVLLAEAtgarvhicHVSTAGSVeliRWAKALGIKVTAEVTPHHLLLTDEDLL--TYDPNYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 217 CLPILKRNTHQLALIEAATSGSKKFfLGTDSAPHAKGAKE-----SACGCAGSYTAHAAV--ELYAE-VFDLEGKIENLe 288
Cdd:PRK09357 276 VNPPLRTEEDREALIEGLKDGTIDA-IATDHAPHAREEKEcefeaAPFGITGLETALSLLytTLVKTgLLDLEQLLEKM- 353
|
330 340 350
....*....|....*....|....*....|....*....
gi 497531564 289 afaSHNGPDFYGMPR------NADTITLV--KEEWNVAE 319
Cdd:PRK09357 354 ---TINPARILGLPAgplaegEPADLVIFdpEAEWTVDG 389
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
173-281 |
4.22e-03 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 38.70 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497531564 173 HITTADAATFVKN---ANENVAATITAHHLLYNRN--HMLVGGIKphfyCLPILKRNTHQLALIEAATSGsKKFFLGTDS 247
Cdd:PRK09236 236 HISTAKELSLFENgplAEKRITAEVCVHHLWFDDSdyARLGNLIK----CNPAIKTASDREALRQALADD-RIDVIATDH 310
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 497531564 248 APHAKGAKESACGCAGS------YTAHAAVELYAE-VFDLE 281
Cdd:PRK09236 311 APHTWEEKQGPYFQAPSglplvqHALPALLELVHEgKLSLE 351
|
|
| |
