|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
1-344 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 720.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 1 MSDRLTLLRPDDWHIHLRDGAALANTVGDAARTFGRAIVMPNLVPPVRNAAEADAYRQRILAARPAASRFEPLMVLYLTD 80
Cdd:COG0418 1 MMQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 81 RTSTEEIRTAKASGFVHAAKLYPAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIDEHLR 160
Cdd:COG0418 81 NTTPEEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 161 RVVERFPTLKVVFEHITTGDAAQFVREAPANVGATITAHHLLYNRNHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGN 240
Cdd:COG0418 161 PLRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 241 PKFFLGTDSAPHARHAKEAACGCAGCYSAYAAIELYAEAFEQRNALDKLEGFASLHGPDFYGLPRNTDRITLVREEWQAP 320
Cdd:COG0418 241 PKFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVP 320
|
330 340
....*....|....*....|....
gi 489203801 321 ASLPFGDFDVVPLRAGETLRWKLL 344
Cdd:COG0418 321 ESIPFGDDTLVPFRAGETLNWRVV 344
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
4-345 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 568.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 4 RLTLLRPDDWHIHLRDGAALANTVGDAARTFGRAIVMPNLVPPVRNAAEADAYRQRILAARPAASRFEPLMVLYLTDRTS 83
Cdd:PLN02599 22 ELTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDNTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 84 TEEIRTAKASGFVHAAKLYPAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIDEHLRRVV 163
Cdd:PLN02599 102 PEEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAPLV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 164 ERFPTLKVVFEHITTGDAAQFVREAPA-NVGATITAHHLLYNRNHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGNPK 242
Cdd:PLN02599 182 QKLPQLKIVMEHITTMDAVEFVESCGDgNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGSKK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 243 FFLGTDSAPHARHAKEAACGCAGCYSAYAAIELYAEAFEQRNALDKLEGFASLHGPDFYGLPRNTDRITLVREEWQAPAS 322
Cdd:PLN02599 262 FFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVPEA 341
|
330 340
....*....|....*....|...
gi 489203801 323 LPFGDFDVVPLRAGETLRWKLLE 345
Cdd:PLN02599 342 YSFGGGTVVPMFAGETIPWSVVS 364
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
5-341 |
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: 531.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 5 LTLLRPDDWHIHLRDGAALANTVGDAARTFGRAIVMPNLVPPVRNAAEADAYRQRILAARPAaSRFEPLMVLYLTDRTST 84
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADPG-PNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 85 EEIRTAKASGFVHAAKLYPAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIdEHLRRVVE 164
Cdd:cd01294 80 EELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 165 RFPTLKVVFEHITTGDAAQFVREAPANVGATITAHHLLYNRNHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGNPKFF 244
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 245 LGTDSAPHARHAKEAACGCAGCYSAYAAIELYAEAFEQRNALDKLEGFASLHGPDFYGLPRNTDRITLVREEWQAPASLP 324
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIP 318
|
330
....*....|....*..
gi 489203801 325 FGDFDVVPLRAGETLRW 341
Cdd:cd01294 319 FGNNGVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
5-343 |
1.03e-172 |
|
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: 483.55 E-value: 1.03e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 5 LTLLRPDDWHIHLRDGAALANTVGDAARTFGRAIVMPNLVPPVRNAAEADAYRQRILAARPAASRFEPLMVLYLTDRTST 84
Cdd:TIGR00856 2 LTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 85 EEIRTAKASGFVHAAKLYPAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIDEHLRRVVE 164
Cdd:TIGR00856 82 EELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 165 RFPTLKVVFEHITTGDAAQFVREAPANVGATITAHHLLYNRNHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGNPKFF 244
Cdd:TIGR00856 162 RFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKFF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 245 LGTDSAPHARHAKEAACGCAGCYSAYAAIELYAEAFEQRNALDKLEGFASLHGPDFYGLPRNTDRITLVREEWQAPASLP 324
Cdd:TIGR00856 242 LGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESIA 321
|
330
....*....|....*....
gi 489203801 325 FGDFDVVPLRAGETLRWKL 343
Cdd:TIGR00856 322 LTDDTLVPFRAGETLSWSV 340
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
12-311 |
1.57e-09 |
|
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: 58.28 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRDGAALANTV-GDAARTFGRAIVMPNL-----------------VPPVRNAAEADAYRQRILAARPAASRFEPL 73
Cdd:pfam01979 8 DAHVHLEMGLLRGIPVpPEFAYEALRLGITTMLksgtttvldmgattstgIEALLEAAEELPLGLRFLGPGCSLDTDGEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 74 MVLYLTDRTSTEEIRTAKA-SGFVHAAKLYPAGATTNSDsgvtriDNIFEALEAMAEVGMPLLVHGEVTRAEvdVFDREK 152
Cdd:pfam01979 88 EGRKALREKLKAGAEFIKGmADGVVFVGLAPHGAPTFSD------DELKAALEEAKKYGLPVAIHALETKGE--VEDAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 153 QFIDEHLRR-VVER------FPTLKVVFEHITTgdaaqfvreaPANVGATITAHHLlynRNHMLVggirphFYCLPILKR 225
Cdd:pfam01979 160 AFGGGIEHGtHLEVaesgglLDIIKLILAHGVH----------LSPTEANLLAEHL---KGAGVA------HCPFSNSKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 226 NTHQEALLDAAVSGNpKFFLGTDSAPHARHAKEAACGcagcysayaaIELYAEAFEQRNALDKLEGF--ASLHGPDFYGL 303
Cdd:pfam01979 221 RSGRIALRKALEDGV-KVGLGTDGAGSGNSLNMLEEL----------RLALELQFDPEGGLSPLEALrmATINPAKALGL 289
|
....*...
gi 489203801 304 PRNTDRIT 311
Cdd:pfam01979 290 DDKVGSIE 297
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
1-344 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 720.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 1 MSDRLTLLRPDDWHIHLRDGAALANTVGDAARTFGRAIVMPNLVPPVRNAAEADAYRQRILAARPAASRFEPLMVLYLTD 80
Cdd:COG0418 1 MMQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 81 RTSTEEIRTAKASGFVHAAKLYPAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIDEHLR 160
Cdd:COG0418 81 NTTPEEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 161 RVVERFPTLKVVFEHITTGDAAQFVREAPANVGATITAHHLLYNRNHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGN 240
Cdd:COG0418 161 PLRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 241 PKFFLGTDSAPHARHAKEAACGCAGCYSAYAAIELYAEAFEQRNALDKLEGFASLHGPDFYGLPRNTDRITLVREEWQAP 320
Cdd:COG0418 241 PKFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVP 320
|
330 340
....*....|....*....|....
gi 489203801 321 ASLPFGDFDVVPLRAGETLRWKLL 344
Cdd:COG0418 321 ESIPFGDDTLVPFRAGETLNWRVV 344
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
4-345 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 568.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 4 RLTLLRPDDWHIHLRDGAALANTVGDAARTFGRAIVMPNLVPPVRNAAEADAYRQRILAARPAASRFEPLMVLYLTDRTS 83
Cdd:PLN02599 22 ELTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDNTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 84 TEEIRTAKASGFVHAAKLYPAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIDEHLRRVV 163
Cdd:PLN02599 102 PEEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAPLV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 164 ERFPTLKVVFEHITTGDAAQFVREAPA-NVGATITAHHLLYNRNHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGNPK 242
Cdd:PLN02599 182 QKLPQLKIVMEHITTMDAVEFVESCGDgNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGSKK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 243 FFLGTDSAPHARHAKEAACGCAGCYSAYAAIELYAEAFEQRNALDKLEGFASLHGPDFYGLPRNTDRITLVREEWQAPAS 322
Cdd:PLN02599 262 FFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVPEA 341
|
330 340
....*....|....*....|...
gi 489203801 323 LPFGDFDVVPLRAGETLRWKLLE 345
Cdd:PLN02599 342 YSFGGGTVVPMFAGETIPWSVVS 364
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
5-341 |
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: 531.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 5 LTLLRPDDWHIHLRDGAALANTVGDAARTFGRAIVMPNLVPPVRNAAEADAYRQRILAARPAaSRFEPLMVLYLTDRTST 84
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADPG-PNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 85 EEIRTAKASGFVHAAKLYPAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIdEHLRRVVE 164
Cdd:cd01294 80 EELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 165 RFPTLKVVFEHITTGDAAQFVREAPANVGATITAHHLLYNRNHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGNPKFF 244
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 245 LGTDSAPHARHAKEAACGCAGCYSAYAAIELYAEAFEQRNALDKLEGFASLHGPDFYGLPRNTDRITLVREEWQAPASLP 324
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIP 318
|
330
....*....|....*..
gi 489203801 325 FGDFDVVPLRAGETLRW 341
Cdd:cd01294 319 FGNNGVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
5-343 |
1.03e-172 |
|
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: 483.55 E-value: 1.03e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 5 LTLLRPDDWHIHLRDGAALANTVGDAARTFGRAIVMPNLVPPVRNAAEADAYRQRILAARPAASRFEPLMVLYLTDRTST 84
Cdd:TIGR00856 2 LTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 85 EEIRTAKASGFVHAAKLYPAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIDEHLRRVVE 164
Cdd:TIGR00856 82 EELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 165 RFPTLKVVFEHITTGDAAQFVREAPANVGATITAHHLLYNRNHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGNPKFF 244
Cdd:TIGR00856 162 RFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKFF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 245 LGTDSAPHARHAKEAACGCAGCYSAYAAIELYAEAFEQRNALDKLEGFASLHGPDFYGLPRNTDRITLVREEWQAPASLP 324
Cdd:TIGR00856 242 LGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESIA 321
|
330
....*....|....*....
gi 489203801 325 FGDFDVVPLRAGETLRWKL 343
Cdd:TIGR00856 322 LTDDTLVPFRAGETLSWSV 340
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
38-305 |
1.84e-11 |
|
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: 64.73 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 38 IVMPNLVPPVRNAAEADAYRQRilAARPAASRFEPLMVLYLTDRTSTEEIRTAKASGFVhAAKLYpagatTNSDSGVTRI 117
Cdd:COG0044 86 VDMPNTNPVTDTPEALEFKLAR--AEEKALVDVGPHGALTKGLGENLAELGALAEAGAV-AFKVF-----MGSDDGNPVL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 118 DN--IFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQF-IDEHLR---RVVERFPTLKVV-----------FEHITTGD 180
Cdd:COG0044 158 DDglLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTsPRLGLKgrpAEAEEEAVARDIalaeetgarlhIVHVSTAE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 181 AAQFVREAPANvGATITA----HHLLYNrnHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGNPKFfLGTDSAPHARHA 256
Cdd:COG0044 238 AVELIREAKAR-GLPVTAevcpHHLTLT--DEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDV-IATDHAPHTLEE 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489203801 257 K-----EAACGCAGCYSAYAAieLYAEAFEQRNaLDkLEGFASL--HGP-DFYGLPR 305
Cdd:COG0044 314 KelpfaEAPNGIPGLETALPL--LLTELVHKGR-LS-LERLVELlsTNPaRIFGLPR 366
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
12-259 |
2.45e-11 |
|
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: 64.28 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRDG-------------AALAN---TVGDaartfgraivMPNLVPPVRNAaeaDAYRQRILAARpAASRFEPLMV 75
Cdd:cd01318 10 DIHVHFREPgltykedfvsgsrAAAAGgvtTVMD----------MPNTKPPTTTA---EALYEKLRLAA-AKSVVDYGLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 76 LYLTDRTSTEEIRTAKASGFvhaaKLYPaGATTNSDSgvtRIDNIFEALEAMAEVgmPLLVHGEVTRAevdVFDREKQFI 155
Cdd:cd01318 76 FGVTGSEDLEELDKAPPAGY----KIFM-GDSTGDLL---DDEETLERIFAEGSV--LVTFHAEDEDR---LRENRKELK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 156 DEHLRRV----------------VERFPTLKVVFEHITTGDAAQFVREAPANVGATITAHHLLYNRNHmlVGGIRPHFYC 219
Cdd:cd01318 143 GESAHPRirdaeaaavataralkLARRHGARLHICHVSTPEELKLIKKAKPGVTVEVTPHHLFLDVED--YDRLGTLGKV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489203801 220 LPILKRNTHQEALLDAAVSGNPKfFLGTDSAPHARHAKEA 259
Cdd:cd01318 221 NPPLRSREDRKALLQALADGRID-VIASDHAPHTLEEKRK 259
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
12-257 |
8.08e-10 |
|
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: 59.76 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRD-----------GAALAntvgdAARTFGRAIVMPNLVPPVRNAAEADaYRQRILAARpAASRFEPlmVLYLTD 80
Cdd:TIGR00857 43 DLHVHLRDpgeeykediesGSKAA-----AHGGFTTVADMPNTKPPIDTPETLE-WKLQRLKKV-SLVDVHL--YGGVTQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 81 RTSTEEIRTAKASGFVHAAklypAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEvtraEVDVFDREKQFIDE--- 157
Cdd:TIGR00857 114 GNQGKELTEAYELKEAGAV----GRMFTDDGSEVQDILSMRRALEYAAIAGVPIALHAE----DPDLIYGGVMHEGPsaa 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 158 --------------HLRRVVERFPTL--KVVFEHITTGDAAQ---FVREAPANVGATITAHHLLYNRNHmlVGGIRPHFY 218
Cdd:TIGR00857 186 qlglparppeaeevAVARLLELAKHAgcPVHICHISTKESLElivKAKSQGIKITAEVTPHHLLLSEED--VARLDGNGK 263
|
250 260 270
....*....|....*....|....*....|....*....
gi 489203801 219 CLPILKRNTHQEALLDAAVSGNPKFFlGTDSAPHARHAK 257
Cdd:TIGR00857 264 VNPPLREKEDRLALIEGLKDGIIDII-ATDHAPHTLEEK 301
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
12-311 |
1.57e-09 |
|
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: 58.28 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRDGAALANTV-GDAARTFGRAIVMPNL-----------------VPPVRNAAEADAYRQRILAARPAASRFEPL 73
Cdd:pfam01979 8 DAHVHLEMGLLRGIPVpPEFAYEALRLGITTMLksgtttvldmgattstgIEALLEAAEELPLGLRFLGPGCSLDTDGEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 74 MVLYLTDRTSTEEIRTAKA-SGFVHAAKLYPAGATTNSDsgvtriDNIFEALEAMAEVGMPLLVHGEVTRAEvdVFDREK 152
Cdd:pfam01979 88 EGRKALREKLKAGAEFIKGmADGVVFVGLAPHGAPTFSD------DELKAALEEAKKYGLPVAIHALETKGE--VEDAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 153 QFIDEHLRR-VVER------FPTLKVVFEHITTgdaaqfvreaPANVGATITAHHLlynRNHMLVggirphFYCLPILKR 225
Cdd:pfam01979 160 AFGGGIEHGtHLEVaesgglLDIIKLILAHGVH----------LSPTEANLLAEHL---KGAGVA------HCPFSNSKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 226 NTHQEALLDAAVSGNpKFFLGTDSAPHARHAKEAACGcagcysayaaIELYAEAFEQRNALDKLEGF--ASLHGPDFYGL 303
Cdd:pfam01979 221 RSGRIALRKALEDGV-KVGLGTDGAGSGNSLNMLEEL----------RLALELQFDPEGGLSPLEALrmATINPAKALGL 289
|
....*...
gi 489203801 304 PRNTDRIT 311
Cdd:pfam01979 290 DDKVGSIE 297
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
12-257 |
3.94e-09 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 57.56 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRDGAALAN---TVGDAARTFGRA---IVMPNLVPPVRN-AAEADAYRqriLAARPAASRFEplmvLYLTDRTST 84
Cdd:PRK01211 50 DIHVHFRTPGETEKedfSTGTLSAIFGGTtfiMDMPNNNIPIKDyNAFSDKLG---RVAPKAYVDFS----LYSMETGNN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 85 EEIRTAKASGFvhaaKLYpAGATTNSDSgvTRIDNifEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIDEHLRR--- 161
Cdd:PRK01211 123 ALILDERSIGL----KVY-MGGTTNTNG--TDIEG--GEIKKINEANIPVFFHAELSECLRKHQFESKNLRDHDLARpie 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 162 ----VVERFPTLKV---VFEHITTGDA-AQFVREApanvgatiTAHHLLYNRNHML--VGGIRPhfyclPILKRNThQEA 231
Cdd:PRK01211 194 ceikAVKYVKNLDLktkIIAHVSSIDViGRFLREV--------TPHHLLLNDDMPLgsYGKVNP-----PLRDRWT-QER 259
|
250 260
....*....|....*....|....*.
gi 489203801 232 LLDAAVSGNPKfFLGTDSAPHARHAK 257
Cdd:PRK01211 260 LLEEYISGRFD-ILSSDHAPHTEEDK 284
|
|
| LigW |
COG2159 |
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ... |
12-175 |
1.94e-08 |
|
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];
Pssm-ID: 441762 [Multi-domain] Cd Length: 253 Bit Score: 54.60 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRDGAALANTVgDAARTfGRAIVMPNLVPPVRNAAEADAYRQRILA-ARPAASRFEPLMVLYLTD-RTSTEEIRT 89
Cdd:COG2159 5 DVHTHLGTPEERLADM-DEAGI-DKAVLSPTPLADPELAALARAANDWLAElVARYPDRFIGFATVDPQDpDAAVEELER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 90 A-KASGFVhAAKLYPagattnsDSGVTRIDN--IFEALEAMAEVGMPLLVHGEVTRAEVDVFDREkQFIDEHLRRVVERF 166
Cdd:COG2159 83 AvEELGFR-GVKLHP-------AVGGFPLDDprLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLY-YAAPLILSGVAERF 153
|
....*....
gi 489203801 167 PTLKVVFEH 175
Cdd:COG2159 154 PDLKFILAH 162
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
12-260 |
9.37e-08 |
|
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: 53.01 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRD-----------GAALAntvgdAARTFGRAIVMPNLVPPVRNAAEADAYRQRilaARPAA-SRFEPLMVLylt 79
Cdd:cd01317 18 DLHVHLREpgfeyketlesGAKAA-----AAGGFTTVVCMPNTNPVIDNPAVVELLKNR---AKDVGiVRVLPIGAL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 80 drtsTEEIRTAKASGFvhaAKLYPAGATTNSDSGVTRIDN--IFEALEAMAEVGMPLLVH--------------GEVTR- 142
Cdd:cd01317 87 ----TKGLKGEELTEI---GELLEAGAVGFSDDGKPIQDAelLRRALEYAAMLDLPIIVHpedpslagggvmneGKVASr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 143 ---------AEVDVFDREKqfidehlrRVVERFPTlKVVFEHITTGDAAQFVREAPA---NVGATITAHHLLYNRNhmLV 210
Cdd:cd01317 160 lglpgippeAETIMVARDL--------ELAEATGA-RVHFQHLSTARSLELIRKAKAkglPVTAEVTPHHLLLDDE--AL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489203801 211 GGIRPHFYCLPILKRNTHQEALLDAAVSGnPKFFLGTDSAPHARHAKEAA 260
Cdd:cd01317 229 ESYDTNAKVNPPLRSEEDREALIEALKDG-TIDAIASDHAPHTDEEKDLP 277
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
12-258 |
1.53e-07 |
|
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: 52.39 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRDGAaLANTVGD-----AARTFG---RAIVMPNLVPPVRNA-AEADAYRQRILAARPAASRFeplmvLYLTDRT 82
Cdd:cd01302 9 DIHVHLRDPG-GTTYKEDfesgsRAAAAGgvtTVIDMPNTGPPPIDLpAIELKIKLAEESSYVDFSFH-----AGIGPGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 83 STEEIRTAKASGFVhAAKLYpaGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEvtraevdvfdREKQFIDEHLRRV 162
Cdd:cd01302 83 VTDELKKLFDAGIN-SLKVF--MNYYFGELFDVDDGTLMRTFLEIASRGGPVMVHAE----------RAAQLAEEAGANV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 163 verfptlKVVfeHITTGDA---AQFVREAPANVGATITAHHLLYNRNHMLVGGirPHFYCLPILKRNTHQEALLDAAVSG 239
Cdd:cd01302 150 -------HIA--HVSSGEAlelIKFAKNKGVKVTCEVCPHHLFLDESMLRLNG--AWGKVNPPLRSKEDREALWEGVKNG 218
|
250
....*....|....*....
gi 489203801 240 NPKFFlGTDSAPHARHAKE 258
Cdd:cd01302 219 KIDTI-ASDHAPHSKEEKE 236
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
12-259 |
4.15e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 45.19 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRD-----------GAALAntvgdAARTFGRAIVMPNLVPPVRNAAEADAYRQRilAARPAASRFEPlmVLYLTD 80
Cdd:PRK09357 57 DLHVHLREpgqedketietGSRAA-----AAGGFTTVVAMPNTKPVIDTPEVVEYVLDR--AKEAGLVDVLP--VGAITK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 81 RTSTEEIrtakasgfVHAAKLYPAGATTNSDSGVTRIDN--IFEALEAMAEVGMPLLVHGEVTRaevdvfDREKQFIDEH 158
Cdd:PRK09357 128 GLAGEEL--------TEFGALKEAGVVAFSDDGIPVQDArlMRRALEYAKALDLLIAQHCEDPS------LTEGGVMNEG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 159 LRRVVERFPTLKVVFE---------------------HITTGDAAQFVREAPA---NVGATITAHHLLYNRNHMLvgGIR 214
Cdd:PRK09357 194 EVSARLGLPGIPAVAEevmiardvllaeatgarvhicHVSTAGSVELIRWAKAlgiKVTAEVTPHHLLLTDEDLL--TYD 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489203801 215 PHFYCLPILKRNTHQEALLDAAVSGNPKFfLGTDSAPHARHAKEA 259
Cdd:PRK09357 272 PNYKVNPPLRTEEDREALIEGLKDGTIDA-IATDHAPHAREEKEC 315
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
12-253 |
6.82e-04 |
|
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: 40.78 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRDGA----------------------ALANTVGDAARTFG--RAIVMPNLVPPVRNAAEADAYRQRILAARPAA 67
Cdd:cd01292 3 DTHVHLDGSAlrgtrlnlelkeaeelspedlyEDTLRALEALLAGGvtTVVDMGSTPPPTTTKAAIEAVAEAARASAGIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 68 SRF--EPLMVLYLTDRTSTEEIRTAKASGF---VHAAKLYPAGATTNSDSgvtriDNIFEALEAMAEVGMPLLVHGEVTr 142
Cdd:cd01292 83 VVLglGIPGVPAAVDEDAEALLLELLRRGLelgAVGLKLAGPYTATGLSD-----ESLRRVLEEARKLGLPVVIHAGEL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 143 aevdvfdrekQFIDEHLRRVVER-FPTLKVVFEHITTGDAAQFVREAPANVGATITAHHLLYNRNHMlvGGIRPhfyclp 221
Cdd:cd01292 157 ----------PDPTRALEDLVALlRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDG--EGAEA------ 218
|
250 260 270
....*....|....*....|....*....|..
gi 489203801 222 ilkrnthqealLDAAVSGNPKFFLGTDSAPHA 253
Cdd:cd01292 219 -----------LRRLLELGIRVTLGTDGPPHP 239
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
12-271 |
7.30e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 41.29 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 12 DWHIHLRDGAA----LANTVGDAARTFGRAIV--MPNLVPPVRNAaeaDAYRQRILAARPAASRFEPLMVLYltdRTSTE 85
Cdd:PRK04250 51 DVHVHLRDFEEsykeTIESGTKAALHGGITLVfdMPNTKPPIMDE---KTYEKRMRIAEKKSYADYALNFLI---AGNCE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 86 EIRTAKAsgfvhaaKLYPA--GATTnsdsGVTRIDNIFEALEAMAEVgmpLLVHGEVTRAEVDVFDREKQFIDEHLRRVV 163
Cdd:PRK04250 125 KAEEIKA-------DFYKIfmGAST----GGIFSENFEVDYACAPGI---VSVHAEDPELIREFPERPPEAEVVAIERAL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 164 ERFPTLKVVFE--HITTGDAAQFVREA-PANVGATITAHHLLYNRNHMLVGgirPHFYCLPILKRNTHQEALLDaAVSGN 240
Cdd:PRK04250 191 EAGKKLKKPLHicHISTKDGLKLILKSnLPWVSFEVTPHHLFLTRKDYERN---PLLKVYPPLRSEEDRKALWE-NFSKI 266
|
250 260 270
....*....|....*....|....*....|..
gi 489203801 241 PkfFLGTDSAPHARHAKEA-ACGCAGCYSAYA 271
Cdd:PRK04250 267 P--IIASDHAPHTLEDKEAgAAGIPGLETEVP 296
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
2-259 |
6.10e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 38.48 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 2 SDRLTLLRPDDWHIHLRD-GAALANT-----VGDAARTFGRAIVMPNLVPPVrnaAEADAYRQR-ILAARPAASRF---- 70
Cdd:PRK02382 48 RGMLLLPGGIDVHVHFREpGYTHKETwytgsRSAAAGGVTTVVDQPNTDPPT---VDGESFDEKaELAARKSIVDFging 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 71 ------EPLMVLYLTDRTSTEEIRTAKASGfvhaaklypagattnsDSGVTRiDNIFEALEAMAEVGMPLLVHGEvtraE 144
Cdd:PRK02382 125 gvtgnwDPLESLWERGVFALGEIFMADSTG----------------GMGIDE-ELFEEALAEAARLGVLATVHAE----D 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489203801 145 VDVFDREKQFI------DEHLR--------RVVERfpTLKVV--------FEHITTGDAAQFVREApanvGAT--ITAHH 200
Cdd:PRK02382 184 EDLFDELAKLLkgdadaDAWSAyrpaaaeaAAVER--ALEVAsetgarihIAHISTPEGVDAARRE----GITceVTPHH 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489203801 201 LLYNRNHMlvGGIRPHFYCLPILKRNTHQEALLDAAVSGNPKfFLGTDSAPHARHAKEA 259
Cdd:PRK02382 258 LFLSRRDW--ERLGTFGKMNPPLRSEKRREALWERLNDGTID-VVASDHAPHTREEKDA 313
|
|
| |
