|
Name |
Accession |
Description |
Interval |
E-value |
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
3-332 |
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: 519.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 3 LKIPGLADMHVHLRQDNMLKAVVPTVAEGGvSVAYVMPNLIPPITTVDACLQYKKEIEQLD--SKTTYLMSLYLSPETTP 80
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGF-SRAIVMPNLKPPVTTTADALAYRERILAADpgPNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 81 EVIYEAAKK-GIRGVKSYPKGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVPPSkDNTVFTAEPKFLPTLLDLHQ 159
Cdd:cd01294 80 EELREAKKKgGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDF-KIDVLDREAKFIPVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 160 RFPKLKIVLEHCTTADAVEAVKACGESVAGTITAHHLYLTQKDWQDD---PYCFCKPVAKTERDRRALIEAATSKNPKFF 236
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGglnPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 237 FGSDSAPHPRSSKLKTPPAAGVFTQPFAASYLAEVFDKEGRLDALKDFACIFGRKFYCIPldFKESNIVLKKESFRVPES 316
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLP--PNKKTITLVKEPWKVPEK 316
|
330
....*....|....*....
gi 19115483 317 VA---NDLVPFHPNEVLQW 332
Cdd:cd01294 317 IPfgnNGVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
10-332 |
8.25e-116 |
|
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: 338.71 E-value: 8.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 10 DMHVHLRQDNMLKAVVPTVAEGgVSVAYVMPNLIPPITTVDACLQYKKEIEQLDSK---TTYLMSLYLSPETTPEVIYEA 86
Cdd:TIGR00856 9 DWHLHLRDGAMLKAVLPYTSEI-FSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAghdFTPLMTLYLTDSLTPEELERA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 87 AKK-GIRGVKSYPKGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVPPSkDNTVFTAEPKFLPTLLD-LHQRFPKL 164
Cdd:TIGR00856 88 KNEgVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHG-DIDIFDREARFIESVLEpLRQRFPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 165 KIVLEHCTTADAVEAVKACGESVAGTITAHHLYLTQKDW---QDDPYCFCKPVAKTERDRRALIEAATSKNPKFFFGSDS 241
Cdd:TIGR00856 167 KVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLlggGVNPHLYCLPILKRNIHQQALLELAASGFPKFFLGTDS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 242 APHPRSSKLKTPPAAGVFTQPFAASYLAEVFDKEGRLDALKDFACIFGRKFYCIPLDFKEsnIVLKKESFRVPESVA--- 318
Cdd:TIGR00856 247 APHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTK--IELVKKEQQIPESIAltd 324
|
330
....*....|....
gi 19115483 319 NDLVPFHPNEVLQW 332
Cdd:TIGR00856 325 DTLVPFRAGETLSW 338
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
1-332 |
3.50e-94 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 284.34 E-value: 3.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 1 MSLKIPGLADMHVHLRQDNMLKAVVPTVAeGGVSVAYVMPNLIPPITTVDACLQYKKEIEQL---DSKTTYLMSLYLSPE 77
Cdd:PLN02599 21 TELTITRPDDWHLHLRDGAKLAAVVPHSA-RHFGRAIVMPNLKPPVTTTARALAYRERIMKAlppGSSFEPLMTLYLTDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 78 TTPEVIYEAAKKG-IRGVKSYPKGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVP-PSKDntVFTAEPKFLPTLL 155
Cdd:PLN02599 100 TTPEEIKAAKASGvVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTdPSVD--IFDREKVFIDTIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 156 -DLHQRFPKLKIVLEHCTTADAVEAVKACGE-SVAGTITAHHLYLT-----QKDWQddPYCFCKPVAKTERDRRALIEAA 228
Cdd:PLN02599 178 aPLVQKLPQLKIVMEHITTMDAVEFVESCGDgNVAATVTPQHLLLNrnalfQGGLQ--PHNYCLPVLKREIHREALVKAA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 229 TSKNPKFFFGSDSAPHPRSSKLKTPPAAGVFTQPFAASYLAEVFDKEGRLDALKDFACIFGRKFYCIPLDfkESNIVLKK 308
Cdd:PLN02599 256 TSGSKKFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRN--TSTITLVK 333
|
330 340
....*....|....*....|....*..
gi 19115483 309 ESFRVPESVA---NDLVPFHPNEVLQW 332
Cdd:PLN02599 334 SAWKVPEAYSfggGTVVPMFAGETIPW 360
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-256 |
1.39e-16 |
|
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: 80.14 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 5 IPGLADMHVHLRQDNMlkavvpTVAE-----------GGV-SVAyVMPNLIPPITTVDAcLQYKKEIEQLDSKTTYLMSL 72
Cdd:COG0044 49 LPGLIDLHVHLREPGL------EHKEdietgtraaaaGGVtTVV-DMPNTNPVTDTPEA-LEFKLARAEEKALVDVGPHG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 73 YLSPETTPEV--IYEAAKKGIRGVKSYpkgATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVPPSKDNTVFTAEPkf 150
Cdd:COG0044 121 ALTKGLGENLaeLGALAEAGAVAFKVF---MGSDDGNPVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGK-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 151 LPTLLDLHQRfP--------------------KLKIVleHCTTADAVEAV---KACGESVAGTITAHHLYLTQKDWQD-D 206
Cdd:COG0044 196 TSPRLGLKGR-PaeaeeeavardialaeetgaRLHIV--HVSTAEAVELIreaKARGLPVTAEVCPHHLTLTDEDLERyG 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115483 207 PYCFCKPVAKTERDRRALIEA-------AtsknpkffFGSDSAPHPRSSKLKTPPAA 256
Cdd:COG0044 273 TNFKVNPPLRTEEDREALWEGladgtidV--------IATDHAPHTLEEKELPFAEA 321
|
|
| Amidohydro_2 |
pfam04909 |
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979. |
76-293 |
7.87e-08 |
|
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
Pssm-ID: 428190 [Multi-domain] Cd Length: 283 Bit Score: 52.92 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 76 PETTPEVIYEAAKKGIRGVKSYPkgattnSESGVESYEP--FYPTFAAMQETGMILNIHgevpPSKDNTVFTAEPKFLPT 153
Cdd:pfam04909 89 EDAAAELERAVGEAGFRGVRLNP------HPGGDPLLGDrlDRPIYEALEELGLPVDIH----TGFGDRPEDTRAIQPLL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 154 LLDLHQRFPKLKIVLEHC---------TTADAVEAVKACgESVAGTITAhhlyLTQKDWQDDPYCFCKPVakterdrRAL 224
Cdd:pfam04909 159 LAGVARKFPDLKIVLDHGggpwipeglDDPAALALLARR-PNVYVKLSG----LYRDLYFDAPLADRPYL-------ARL 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115483 225 IEAATSKnpKFFFGSDsAPHPrssklktPPAAGVFTQPFAASYLAEVFDKEgrldalkDFACIFG---RKFY 293
Cdd:pfam04909 227 LEAFGPD--RILFGSD-WPHP-------PLEISPDDGVLLDLPLLLALSDE-------EREKILGgnaARLY 281
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
3-332 |
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: 519.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 3 LKIPGLADMHVHLRQDNMLKAVVPTVAEGGvSVAYVMPNLIPPITTVDACLQYKKEIEQLD--SKTTYLMSLYLSPETTP 80
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGF-SRAIVMPNLKPPVTTTADALAYRERILAADpgPNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 81 EVIYEAAKK-GIRGVKSYPKGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVPPSkDNTVFTAEPKFLPTLLDLHQ 159
Cdd:cd01294 80 EELREAKKKgGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDF-KIDVLDREAKFIPVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 160 RFPKLKIVLEHCTTADAVEAVKACGESVAGTITAHHLYLTQKDWQDD---PYCFCKPVAKTERDRRALIEAATSKNPKFF 236
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGglnPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 237 FGSDSAPHPRSSKLKTPPAAGVFTQPFAASYLAEVFDKEGRLDALKDFACIFGRKFYCIPldFKESNIVLKKESFRVPES 316
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLP--PNKKTITLVKEPWKVPEK 316
|
330
....*....|....*....
gi 19115483 317 VA---NDLVPFHPNEVLQW 332
Cdd:cd01294 317 IPfgnNGVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
10-332 |
8.25e-116 |
|
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: 338.71 E-value: 8.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 10 DMHVHLRQDNMLKAVVPTVAEGgVSVAYVMPNLIPPITTVDACLQYKKEIEQLDSK---TTYLMSLYLSPETTPEVIYEA 86
Cdd:TIGR00856 9 DWHLHLRDGAMLKAVLPYTSEI-FSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAghdFTPLMTLYLTDSLTPEELERA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 87 AKK-GIRGVKSYPKGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVPPSkDNTVFTAEPKFLPTLLD-LHQRFPKL 164
Cdd:TIGR00856 88 KNEgVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHG-DIDIFDREARFIESVLEpLRQRFPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 165 KIVLEHCTTADAVEAVKACGESVAGTITAHHLYLTQKDW---QDDPYCFCKPVAKTERDRRALIEAATSKNPKFFFGSDS 241
Cdd:TIGR00856 167 KVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLlggGVNPHLYCLPILKRNIHQQALLELAASGFPKFFLGTDS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 242 APHPRSSKLKTPPAAGVFTQPFAASYLAEVFDKEGRLDALKDFACIFGRKFYCIPLDFKEsnIVLKKESFRVPESVA--- 318
Cdd:TIGR00856 247 APHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTK--IELVKKEQQIPESIAltd 324
|
330
....*....|....
gi 19115483 319 NDLVPFHPNEVLQW 332
Cdd:TIGR00856 325 DTLVPFRAGETLSW 338
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
1-332 |
3.50e-94 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 284.34 E-value: 3.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 1 MSLKIPGLADMHVHLRQDNMLKAVVPTVAeGGVSVAYVMPNLIPPITTVDACLQYKKEIEQL---DSKTTYLMSLYLSPE 77
Cdd:PLN02599 21 TELTITRPDDWHLHLRDGAKLAAVVPHSA-RHFGRAIVMPNLKPPVTTTARALAYRERIMKAlppGSSFEPLMTLYLTDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 78 TTPEVIYEAAKKG-IRGVKSYPKGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVP-PSKDntVFTAEPKFLPTLL 155
Cdd:PLN02599 100 TTPEEIKAAKASGvVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTdPSVD--IFDREKVFIDTIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 156 -DLHQRFPKLKIVLEHCTTADAVEAVKACGE-SVAGTITAHHLYLT-----QKDWQddPYCFCKPVAKTERDRRALIEAA 228
Cdd:PLN02599 178 aPLVQKLPQLKIVMEHITTMDAVEFVESCGDgNVAATVTPQHLLLNrnalfQGGLQ--PHNYCLPVLKREIHREALVKAA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 229 TSKNPKFFFGSDSAPHPRSSKLKTPPAAGVFTQPFAASYLAEVFDKEGRLDALKDFACIFGRKFYCIPLDfkESNIVLKK 308
Cdd:PLN02599 256 TSGSKKFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRN--TSTITLVK 333
|
330 340
....*....|....*....|....*..
gi 19115483 309 ESFRVPESVA---NDLVPFHPNEVLQW 332
Cdd:PLN02599 334 SAWKVPEAYSfggGTVVPMFAGETIPW 360
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
2-256 |
2.83e-17 |
|
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: 81.61 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 2 SLKIPGLADMHVHLRQDNM-LKAVVPT----VAEGGVSVAYVMPNLIPPITTVDAcLQYKKEIEQLDSKTTYLMSLYLSP 76
Cdd:cd01318 2 LLILPGVIDIHVHFREPGLtYKEDFVSgsraAAAGGVTTVMDMPNTKPPTTTAEA-LYEKLRLAAAKSVVDYGLYFGVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 77 ETTPEviyEAAKKGIRGVKSYPkGATTNseSGVESYEPFYPTFAAMQEtgmILNIHGEVPP------------SKDNTVF 144
Cdd:cd01318 81 SEDLE---ELDKAPPAGYKIFM-GDSTG--DLLDDEETLERIFAEGSV---LVTFHAEDEDrlrenrkelkgeSAHPRIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 145 TAEPKFLPTLLDLH--QRFPKLKIVLeHCTTADAVEAVKACGESVAGTITAHHLYLTQKDWQD-DPYCFCKPVAKTERDR 221
Cdd:cd01318 152 DAEAAAVATARALKlaRRHGARLHIC-HVSTPEELKLIKKAKPGVTVEVTPHHLFLDVEDYDRlGTLGKVNPPLRSREDR 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 19115483 222 RALIEAAtsKNPKF-FFGSDSAPHPRSSKLKTPPAA 256
Cdd:cd01318 231 KALLQAL--ADGRIdVIASDHAPHTLEEKRKGYPAA 264
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-256 |
1.39e-16 |
|
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: 80.14 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 5 IPGLADMHVHLRQDNMlkavvpTVAE-----------GGV-SVAyVMPNLIPPITTVDAcLQYKKEIEQLDSKTTYLMSL 72
Cdd:COG0044 49 LPGLIDLHVHLREPGL------EHKEdietgtraaaaGGVtTVV-DMPNTNPVTDTPEA-LEFKLARAEEKALVDVGPHG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 73 YLSPETTPEV--IYEAAKKGIRGVKSYpkgATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVPPSKDNTVFTAEPkf 150
Cdd:COG0044 121 ALTKGLGENLaeLGALAEAGAVAFKVF---MGSDDGNPVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGK-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 151 LPTLLDLHQRfP--------------------KLKIVleHCTTADAVEAV---KACGESVAGTITAHHLYLTQKDWQD-D 206
Cdd:COG0044 196 TSPRLGLKGR-PaeaeeeavardialaeetgaRLHIV--HVSTAEAVELIreaKARGLPVTAEVCPHHLTLTDEDLERyG 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115483 207 PYCFCKPVAKTERDRRALIEA-------AtsknpkffFGSDSAPHPRSSKLKTPPAA 256
Cdd:COG0044 273 TNFKVNPPLRTEEDREALWEGladgtidV--------IATDHAPHTLEEKELPFAEA 321
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
5-244 |
4.70e-14 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 72.49 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 5 IPGLADMHVHLRQ-DNMLKAVVPT----VAEGGVSVAYVMPNLIPPITTVDAclqYKKEIEQLDSKT--TYLMSLYLSPE 77
Cdd:PRK04250 46 LPGLIDVHVHLRDfEESYKETIESgtkaALHGGITLVFDMPNTKPPIMDEKT---YEKRMRIAEKKSyaDYALNFLIAGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 78 TtpeviyEAAKKGIRGVKSYPKGATTnSESGVESYEPFYPTFAAmqetgmILNIHGEVPPSKDNTVF---TAEPKFLPTL 154
Cdd:PRK04250 123 C------EKAEEIKADFYKIFMGAST-GGIFSENFEVDYACAPG------IVSVHAEDPELIREFPErppEAEVVAIERA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 155 LDLHQRFPK-LKIVleHCTTADAVEAV-KACGESVAGTITAHHLYLTQKDWQDDPYCFCKPVAKTERDRRALIEaATSKN 232
Cdd:PRK04250 190 LEAGKKLKKpLHIC--HISTKDGLKLIlKSNLPWVSFEVTPHHLFLTRKDYERNPLLKVYPPLRSEEDRKALWE-NFSKI 266
|
250
....*....|..
gi 19115483 233 PkfFFGSDSAPH 244
Cdd:PRK04250 267 P--IIASDHAPH 276
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
2-256 |
6.99e-13 |
|
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: 69.01 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 2 SLKIPGLADMHVHLRQDNM-----LKAVVPTVAEGGVSVAYVMPNLIPPITTVDAcLQYKKEIEQLDSKTTYLM------ 70
Cdd:TIGR00857 35 LLVLPGFIDLHVHLRDPGEeykedIESGSKAAAHGGFTTVADMPNTKPPIDTPET-LEWKLQRLKKVSLVDVHLyggvtq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 71 SLYLSPETTPEVIYEAAKKGIRGVKSYpkgattnseSGVESYEPFYPTFAAMQETGMILNIHGEvppskDNTVFTAEPKF 150
Cdd:TIGR00857 114 GNQGKELTEAYELKEAGAVGRMFTDDG---------SEVQDILSMRRALEYAAIAGVPIALHAE-----DPDLIYGGVMH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 151 ---LPTLLDLHQRFPK-----LKIVLE------------HCTTADAVEAV---KACGESVAGTITAHHLYLTQKDWQD-D 206
Cdd:TIGR00857 180 egpSAAQLGLPARPPEaeevaVARLLElakhagcpvhicHISTKESLELIvkaKSQGIKITAEVTPHHLLLSEEDVARlD 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19115483 207 PYCFCKPVAKTERDRRALIEAATSKNPKfFFGSDSAPHPRSSKLKTPPAA 256
Cdd:TIGR00857 260 GNGKVNPPLREKEDRLALIEGLKDGIID-IIATDHAPHTLEEKTKEFAAA 308
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
6-249 |
4.12e-12 |
|
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: 66.26 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 6 PGLADMHVHLRQD--NMLKAVVPT----VAEGGVSVAYVMPNLIPPITTVDACLQYKKEIEQlDSKTTYLMSLYLSPETT 79
Cdd:cd01302 5 PGFIDIHVHLRDPggTTYKEDFESgsraAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEE-SSYVDFSFHAGIGPGDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 80 PEVIYEAAKKGIRGVKSYpkGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVppskdntvftaepkflptLLDLHQ 159
Cdd:cd01302 84 TDELKKLFDAGINSLKVF--MNYYFGELFDVDDGTLMRTFLEIASRGGPVMVHAER------------------AAQLAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 160 RFpKLKIVLEHCTTADAVEAV---KACGESVAGTITAHHLYLTQKDWQDDPYCF-CKPVAKTERDRRALIEAAtsKNPKF 235
Cdd:cd01302 144 EA-GANVHIAHVSSGEALELIkfaKNKGVKVTCEVCPHHLFLDESMLRLNGAWGkVNPPLRSKEDREALWEGV--KNGKI 220
|
250
....*....|....*
gi 19115483 236 -FFGSDSAPHPRSSK 249
Cdd:cd01302 221 dTIASDHAPHSKEEK 235
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
2-269 |
3.46e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 60.55 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 2 SLKIPGLADMHVHLR--QDNMLKAVVPTVAE---GGVSVAYVMPNLIPPITTVDACLQYKKEIEQLdSKTTYlmSLYLSP 76
Cdd:PRK00369 43 TLILPGAIDLHVHLRglKLSYKEDVASGTSEaayGGVTLVADMPNTIPPLNTPEAITEKLAELEYY-SRVDY--FVYSGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 77 ETTPEviyEAAKKGIRGVKSYPKgattnsesGVESYEpfypTFAAMQETGMILNIHGEVP-----PSKDNTVFTAEPKFL 151
Cdd:PRK00369 120 TKDPE---KVDKLPIAGYKIFPE--------DLEREE----TFRVLLKSRKLKILHPEVPlalksNRKLRRNCWYEIAAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 152 PTLLDLhqrfPKLKIVleHCTTADAVEAVKACGESVagTITAHHL-YLTQKD--WQDDPycfckPV-AKTERDR--RALI 225
Cdd:PRK00369 185 YYVKDY----QNVHIT--HASNPRTVRLAKELGFTV--DITPHHLlVNGEKDclTKVNP-----PIrDINERLWllQALS 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19115483 226 EAATsknpkffFGSDSAPHPRSSKLKTPP------AAGVFTQPFAASYLA 269
Cdd:PRK00369 252 EVDA-------IASDHAPHSSFEKLQPYEvcppgiAALSFTPPFIYTLVS 294
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
6-260 |
9.11e-10 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 59.61 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 6 PGLADMHVHLRQDNML---------KAVvptvAEGGVSVAYVMP-NLIPPITTVdACLQYKKEIEQLDSKTTYlmSLY-- 73
Cdd:cd01315 52 PGLIDTHVHINEPGRTewegfetgtKAA----AAGGITTIIDMPlNSIPPTTTV-ENLEAKLEAAQGKLHVDV--GFWgg 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 74 LSPETTPEvIYEAAKKGIRGVKSYPkgattnSESGVESY-----EPFYPTFAAMQETGMILNIHGEVPPSKDNTVFTAEP 148
Cdd:cd01315 125 LVPGNLDQ-LRPLDEAGVVGFKCFL------CPSGVDEFpavddEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 149 K-------FLPT------------LLDLHQRFP-KLKIVleHCTTADAVEAVKAC-GESVAGTI-TAHH-LYLTQKDWQD 205
Cdd:cd01315 198 KgkrdyrdYLASrpvfteveaiqrILLLAKETGcRLHIV--HLSSAEAVPLIREArAEGVDVTVeTCPHyLTFTAEDVPD 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115483 206 -DPYCFCKPVAKTERDRRALIEAATSKNPKfFFGSDSAPHPrsSKLKTPPAAGVFT 260
Cdd:cd01315 276 gGTEFKCAPPIRDAANQEQLWEALENGDID-MVVSDHSPCT--PELKLLGKGDFFK 328
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
2-258 |
1.77e-09 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 58.23 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 2 SLKIPGLADMHVHLRQDNM-----LKAVVPTVAEGGVSVAYVMPNLIPPITTVDAcLQYKKEIEQLDSKTTYLMSLYLSP 76
Cdd:cd01316 2 TIRLPGLIDVHVHLREPGAthkedFASGTKAALAGGFTMVRAMPNTNPSIVDVAS-LKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 77 ETTPEViyeaakkgirgvksypkGATTNSESGVEsyepFYP--TFAamqeTGMILNI-----HGEVPPSKDNTVFTAEPK 149
Cdd:cd01316 81 TNAATV-----------------GELASEAVGLK----FYLneTFS----TLILDKItawasHFNAWPSTKPIVTHAKSQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 150 FLPTLL---DLHQRfpklKIVLEHCTTADA---VEAVKACGESVAGTITAHHLYLTQKDWQDDPYcfckPVAK---TERD 220
Cdd:cd01316 136 TLAAVLllaSLHNR----SIHICHVSSKEEinlIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQY----EVRPflpTRED 207
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19115483 221 RRALIEAATSKNpkfFFGSDSAPHP---RSSKLKTPPAAGV 258
Cdd:cd01316 208 QEALWENLDYID---CFATDHAPHTlaeKTGNKPPPGFPGV 245
|
|
| LigW |
COG2159 |
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ... |
10-171 |
1.79e-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: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 10 DMHVHLRQ-DNMLKAVvptvAEGGVSVAYVMPNLIPPITTVDACLQYKKEIEQL--DSKTTYLMSLYLSPETTPEVIYE- 85
Cdd:COG2159 5 DVHTHLGTpEERLADM----DEAGIDKAVLSPTPLADPELAALARAANDWLAELvaRYPDRFIGFATVDPQDPDAAVEEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 86 ---AAKKGIRGVKSYPkgattnSESGVESYEP-FYPTFAAMQETGMILNIHGEVPPSKDNTVftAEPKFLPTLLD-LHQR 160
Cdd:COG2159 81 eraVEELGFRGVKLHP------AVGGFPLDDPrLDPLYEAAAELGLPVLVHPGTPPGPPPGL--DLYYAAPLILSgVAER 152
|
170
....*....|.
gi 19115483 161 FPKLKIVLEHC 171
Cdd:COG2159 153 FPDLKFILAHG 163
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
3-249 |
1.95e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 55.43 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 3 LKIPGLADMHVHLRQDNM-LKAVVPT----VAEGGVSVAYVMPNLIPPITTVDACLQyKKEIEQLDSKTTYLMSLYLSPE 77
Cdd:PRK02382 51 LLLPGGIDVHVHFREPGYtHKETWYTgsrsAAAGGVTTVVDQPNTDPPTVDGESFDE-KAELAARKSIVDFGINGGVTGN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 78 TTP-EVIYEaakkgiRGVKSYpkG----ATTNSESGVESyEPFYPTFAAMQETGMILNIHGEvppskDNTVFTAEPKFLP 152
Cdd:PRK02382 130 WDPlESLWE------RGVFAL--GeifmADSTGGMGIDE-ELFEEALAEAARLGVLATVHAE-----DEDLFDELAKLLK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 153 TLL--DLHQRF-------------------PKLKIVLEHCTTADAVEAVKAcgESVAGTITAHHLYLTQKDWqDDPYCFC 211
Cdd:PRK02382 196 GDAdaDAWSAYrpaaaeaaaveralevaseTGARIHIAHISTPEGVDAARR--EGITCEVTPHHLFLSRRDW-ERLGTFG 272
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19115483 212 K--PVAKTERDRRALIEAATSKNPKfFFGSDSAPHPRSSK 249
Cdd:PRK02382 273 KmnPPLRSEKRREALWERLNDGTID-VVASDHAPHTREEK 311
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
6-279 |
4.73e-08 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 54.05 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 6 PGLADMHVHLRQdnmlkavvP------TVAE-------GGVSVAYVMPNLIPPITTvdaclqykkeieqldskttylmsl 72
Cdd:PRK09357 53 PGLVDLHVHLRE--------PgqedkeTIETgsraaaaGGFTTVVAMPNTKPVIDT------------------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 73 ylsPETTPEVIYEAAKKGIrgVKSYPKGATTNSESGVESYEpfyptFAAMQETG-------------------------- 126
Cdd:PRK09357 101 ---PEVVEYVLDRAKEAGL--VDVLPVGAITKGLAGEELTE-----FGALKEAGvvafsddgipvqdarlmrraleyaka 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 127 --MILNIHGEVPPSKDNTVF----TAEPKFLPT--------------LLDLHQRfPKLKIvlEHCTTADAVEAV---KAC 183
Cdd:PRK09357 171 ldLLIAQHCEDPSLTEGGVMnegeVSARLGLPGipavaeevmiardvLLAEATG-ARVHI--CHVSTAGSVELIrwaKAL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 184 GESVAGTITAHHLYLTQKDWQDDpycfcKPVAK------TERDRRALIEA---------ATsknpkfffgsDSAPHPRSS 248
Cdd:PRK09357 248 GIKVTAEVTPHHLLLTDEDLLTY-----DPNYKvnpplrTEEDREALIEGlkdgtidaiAT----------DHAPHAREE 312
|
330 340 350
....*....|....*....|....*....|....*...
gi 19115483 249 KLKTPPAAgvftqPF-------AASYLAEVFDKEGRLD 279
Cdd:PRK09357 313 KECEFEAA-----PFgitgletALSLLYTTLVKTGLLD 345
|
|
| Amidohydro_2 |
pfam04909 |
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979. |
76-293 |
7.87e-08 |
|
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
Pssm-ID: 428190 [Multi-domain] Cd Length: 283 Bit Score: 52.92 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 76 PETTPEVIYEAAKKGIRGVKSYPkgattnSESGVESYEP--FYPTFAAMQETGMILNIHgevpPSKDNTVFTAEPKFLPT 153
Cdd:pfam04909 89 EDAAAELERAVGEAGFRGVRLNP------HPGGDPLLGDrlDRPIYEALEELGLPVDIH----TGFGDRPEDTRAIQPLL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 154 LLDLHQRFPKLKIVLEHC---------TTADAVEAVKACgESVAGTITAhhlyLTQKDWQDDPYCFCKPVakterdrRAL 224
Cdd:pfam04909 159 LAGVARKFPDLKIVLDHGggpwipeglDDPAALALLARR-PNVYVKLSG----LYRDLYFDAPLADRPYL-------ARL 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115483 225 IEAATSKnpKFFFGSDsAPHPrssklktPPAAGVFTQPFAASYLAEVFDKEgrldalkDFACIFG---RKFY 293
Cdd:pfam04909 227 LEAFGPD--RILFGSD-WPHP-------PLEISPDDGVLLDLPLLLALSDE-------EREKILGgnaARLY 281
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
5-293 |
1.56e-07 |
|
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: 52.12 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 5 IPGLADMHVHLRQDNMLKAVVP--TVAEGGVSVayVMPNLIPPITTVDAC--------LQYKKEIEQLDSKTTYLMS-LY 73
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLRGIPVPpeFAYEALRLG--ITTMLKSGTTTVLDMgattstgiEALLEAAEELPLGLRFLGPgCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 74 LSPETTPEVIYEAAKKGIRGVKSYPKGATTNSESGVESYEPFYPTFAAMQ-------ETGMILNIH-----GEVPPSKDN 141
Cdd:pfam01979 81 LDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKaaleeakKYGLPVAIHaletkGEVEDAIAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 142 TVFTAEPKFLPTLLDLHQRFPKLKIVLEHCTTADAVEAvkacgesvagTITAHHLYltqkdwqDDPYCFC-KPVAKTERD 220
Cdd:pfam01979 161 FGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPTEA----------NLLAEHLK-------GAGVAHCpFSNSKLRSG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115483 221 RRALIEAATSkNPKFFFGSDSAPHPRSSKLKTPPAAGVFTQpfaasylaevFDKEGRLDALK--DFACIFGRKFY 293
Cdd:pfam01979 224 RIALRKALED-GVKVGLGTDGAGSGNSLNMLEELRLALELQ----------FDPEGGLSPLEalRMATINPAKAL 287
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
5-272 |
2.30e-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: 51.85 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 5 IPGLADMHVHLRQDN----------MLKAvvptvAEGGVSVAYVMPNLIPPITTVdACLQYKKEIEQLDSkttyLMSLYL 74
Cdd:cd01317 13 APGLVDLHVHLREPGfeyketlesgAKAA-----AAGGFTTVVCMPNTNPVIDNP-AVVELLKNRAKDVG----IVRVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 75 SPETTPEV-------IYEAAKKGIRGVkSYPKGATTNSE---------SGVESYEPFYPTFAAMQETGMI--------LN 130
Cdd:cd01317 83 IGALTKGLkgeelteIGELLEAGAVGF-SDDGKPIQDAEllrraleyaAMLDLPIIVHPEDPSLAGGGVMnegkvasrLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115483 131 IHGeVPPSkdntvftAEPKFLPTLLDLhQRFPKLKIVLEHCTTADAVEAV---KACGESVAGTITAHHLYLTQKD-WQDD 206
Cdd:cd01317 162 LPG-IPPE-------AETIMVARDLEL-AEATGARVHFQHLSTARSLELIrkaKAKGLPVTAEVTPHHLLLDDEAlESYD 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115483 207 PYCFCKPVAKTERDRRALIEAAtsKNPKF-FFGSDSAPHPRSSKLKTPPAAgvftqPFAASYLAEVF 272
Cdd:cd01317 233 TNAKVNPPLRSEEDREALIEAL--KDGTIdAIASDHAPHTDEEKDLPFAEA-----PPGIIGLETAL 292
|
|
| |
