|
Name |
Accession |
Description |
Interval |
E-value |
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
12-337 |
2.40e-156 |
|
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: 441.34 E-value: 2.40e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 12 ALDMHLHLRDDDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEACKNDEFEPHVTIFFQVDYSYEFLKEI 91
Cdd:cd01294 6 PDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADPGPNFTPLMTLYLTENTTPEELREA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 92 KDE--IIAVKLYPFGVTTNSETGVSsmDVEVLRPTLESMEKLGIPLCVHGETKGF---MMDREKEFLPIYESLAINFPDL 166
Cdd:cd01294 86 KKKggIRGVKLYPAGATTNSQGGVT--DLEKIYPVLEAMQKLGMPLLVHGEVPDFkidVLDREAKFIPVLEPLAQRFPKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 167 KIMMEHISSKESIDLLKKYD-NLYATITVHHLMLTLDDVVGGMLNPHAFCKPIVKKPEDRKALLQLALSAHPKVMFGSDS 245
Cdd:cd01294 164 KIVLEHITTADAVEYVKSCNeNVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFFLGSDS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 246 APHQKNTKECHHGAAGVFTSPIALQVLTQLFEEHGKLDNLNAFISLNAQRIYNLNPIKKEIRLIKKDFIVPEVYSYKSEQ 325
Cdd:cd01294 244 APHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIPFGNNG 323
|
330
....*....|..
gi 2508954854 326 VVPLFAGQKLVW 337
Cdd:cd01294 324 VVPFRAGETLRW 335
|
|
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
14-339 |
1.41e-120 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 350.94 E-value: 1.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEAC-KNDEFEPHVTIFFQVDYSYEFLKEIK 92
Cdd:COG0418 12 DWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALpAGSDFEPLMTLYLTDNTTPEEIARAK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 93 DE--IIAVKLYPFGVTTNSETGVSsmDVEVLRPTLESMEKLGIPLCVHGE-TKG----FmmDREKEFLP-IYESLAINFP 164
Cdd:COG0418 92 ASgvVTAVKLYPAGATTNSDSGVT--DIDKIYPVLEAMQEIGMPLLVHGEvTDPdidiF--DREAVFIDrVLEPLRRRFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 165 DLKIMMEHISSKESIDLLKKY-DNLYATITVHHLMLTLDDVVGGMLNPHAFCKPIVKKPEDRKALLQLALSAHPKVMFGS 243
Cdd:COG0418 168 ELKVVFEHITTKEAVDFVRAAgDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGNPKFFLGT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 244 DSAPHQKNTKECHHGAAGVFTSPIALQVLTQLFEEHGKLDNLNAFISLNAQRIYNLNPIKKEIRLIKKDFIVPEVYSYKS 323
Cdd:COG0418 248 DSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPESIPFGD 327
|
330
....*....|....*.
gi 2508954854 324 EQVVPLFAGQKLVWSI 339
Cdd:COG0418 328 DTLVPFRAGETLNWRV 343
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
14-339 |
2.24e-119 |
|
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: 347.96 E-value: 2.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEAC-KNDEFEPHVTIFFQVDYSYEFLKEIK 92
Cdd:TIGR00856 9 DWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVpAGHDFTPLMTLYLTDSLTPEELERAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 93 DE--IIAVKLYPFGVTTNSETGVSsmDVEVLRPTLESMEKLGIPLCVHGE-TKG--FMMDREKEFLPIY-ESLAINFPDL 166
Cdd:TIGR00856 89 NEgvVRAVKLYPAGATTNSSHGVT--DIDAIMPVLEAMEKIGLPLLLHGEvTHGdiDIFDREARFIESVlEPLRQRFPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 167 KIMMEHISSKESIDLLKKYDN-LYATITVHHLMLTLDDVVGGMLNPHAFCKPIVKKPEDRKALLQLALSAHPKVMFGSDS 245
Cdd:TIGR00856 167 KVVLEHITTKDAIDYVEDGNNrLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKFFLGTDS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 246 APHQKNTKECHHGAAGVFTSPIALQVLTQLFEEHGKLDNLNAFISLNAQRIYNLNPIKKEIRLIKKDFIVPEVYSYKSEQ 325
Cdd:TIGR00856 247 APHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESIALTDDT 326
|
330
....*....|....
gi 2508954854 326 VVPLFAGQKLVWSI 339
Cdd:TIGR00856 327 LVPFRAGETLSWSV 340
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
14-340 |
2.78e-100 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 300.13 E-value: 2.78e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEAC-KNDEFEPHVTIFFQVDYSYEFLKEIK 92
Cdd:PLN02599 30 DWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALpPGSSFEPLMTLYLTDNTTPEEIKAAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 93 DE--IIAVKLYPFGVTTNSETGVSsmDVEVLRPTLESMEKLGIPLCVHGE-TKGF--MMDREKEFLP-IYESLAINFPDL 166
Cdd:PLN02599 110 ASgvVFAVKLYPAGATTNSQAGVT--DLGKCLPVLEEMAEQGMPLLVHGEvTDPSvdIFDREKVFIDtILAPLVQKLPQL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 167 KIMMEHISSKESIDLLK--KYDNLYATITVHHLMLTLDDVVGGMLNPHAFCKPIVKKPEDRKALLQLALSAHPKVMFGSD 244
Cdd:PLN02599 188 KIVMEHITTMDAVEFVEscGDGNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGSKKFFLGTD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 245 SAPHQKNTKECHHGAAGVFTSPIALQVLTQLFEEHGKLDNLNAFISLNAQRIYNLNPIKKEIRLIKKDFIVPEVYSYKSE 324
Cdd:PLN02599 268 SAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVPEAYSFGGG 347
|
330
....*....|....*.
gi 2508954854 325 QVVPLFAGQKLVWSIS 340
Cdd:PLN02599 348 TVVPMFAGETIPWSVV 363
|
|
| Amidohydro_2 |
pfam04909 |
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979. |
14-299 |
3.22e-10 |
|
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
Pssm-ID: 428190 [Multi-domain] Cd Length: 283 Bit Score: 60.24 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTF--AGALIMPNLLP---PITTKEALLAYKKRIQEACK--NDEF------EPHVTIFFq 80
Cdd:pfam04909 2 DAHAHLWPDDERIGFDPGGRLPFmkRRGYDPRDASPedlLALGAALGVARAVVVAASCRgaNNRVaaealaRPGRFLGG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 81 VDYSYEFLKEIKDEIIA---------VKLYPfgvttnSETGVSSMDVEVLRPTLESMEKLGIPLCVHGETKGFMMDREKE 151
Cdd:pfam04909 81 VAVVPLDPEDAAAELERavgeagfrgVRLNP------HPGGDPLLGDRLDRPIYEALEELGLPVDIHTGFGDRPEDTRAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 152 FLPIYESLAINFPDLKIMMEH---------ISSKESIDLLKKYDNLYATITVHHLMLTLDDVVGgmlNPHAFCKPIVKKP 222
Cdd:pfam04909 155 QPLLLAGVARKFPDLKIVLDHgggpwipegLDDPAALALLARRPNVYVKLSGLYRDLYFDAPLA---DRPYLARLLEAFG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2508954854 223 EDRkallqlalsahpkVMFGSDsAPH--QKNTKECHHGAAGVFTSPIALQVLTQLFEEhgkldnlnafislNAQRIYNL 299
Cdd:pfam04909 232 PDR-------------ILFGSD-WPHppLEISPDDGVLLDLPLLLALSDEEREKILGG-------------NAARLYGL 283
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
12-337 |
2.40e-156 |
|
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: 441.34 E-value: 2.40e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 12 ALDMHLHLRDDDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEACKNDEFEPHVTIFFQVDYSYEFLKEI 91
Cdd:cd01294 6 PDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADPGPNFTPLMTLYLTENTTPEELREA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 92 KDE--IIAVKLYPFGVTTNSETGVSsmDVEVLRPTLESMEKLGIPLCVHGETKGF---MMDREKEFLPIYESLAINFPDL 166
Cdd:cd01294 86 KKKggIRGVKLYPAGATTNSQGGVT--DLEKIYPVLEAMQKLGMPLLVHGEVPDFkidVLDREAKFIPVLEPLAQRFPKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 167 KIMMEHISSKESIDLLKKYD-NLYATITVHHLMLTLDDVVGGMLNPHAFCKPIVKKPEDRKALLQLALSAHPKVMFGSDS 245
Cdd:cd01294 164 KIVLEHITTADAVEYVKSCNeNVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFFLGSDS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 246 APHQKNTKECHHGAAGVFTSPIALQVLTQLFEEHGKLDNLNAFISLNAQRIYNLNPIKKEIRLIKKDFIVPEVYSYKSEQ 325
Cdd:cd01294 244 APHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIPFGNNG 323
|
330
....*....|..
gi 2508954854 326 VVPLFAGQKLVW 337
Cdd:cd01294 324 VVPFRAGETLRW 335
|
|
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
14-339 |
1.41e-120 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 350.94 E-value: 1.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEAC-KNDEFEPHVTIFFQVDYSYEFLKEIK 92
Cdd:COG0418 12 DWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALpAGSDFEPLMTLYLTDNTTPEEIARAK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 93 DE--IIAVKLYPFGVTTNSETGVSsmDVEVLRPTLESMEKLGIPLCVHGE-TKG----FmmDREKEFLP-IYESLAINFP 164
Cdd:COG0418 92 ASgvVTAVKLYPAGATTNSDSGVT--DIDKIYPVLEAMQEIGMPLLVHGEvTDPdidiF--DREAVFIDrVLEPLRRRFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 165 DLKIMMEHISSKESIDLLKKY-DNLYATITVHHLMLTLDDVVGGMLNPHAFCKPIVKKPEDRKALLQLALSAHPKVMFGS 243
Cdd:COG0418 168 ELKVVFEHITTKEAVDFVRAAgDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGNPKFFLGT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 244 DSAPHQKNTKECHHGAAGVFTSPIALQVLTQLFEEHGKLDNLNAFISLNAQRIYNLNPIKKEIRLIKKDFIVPEVYSYKS 323
Cdd:COG0418 248 DSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPESIPFGD 327
|
330
....*....|....*.
gi 2508954854 324 EQVVPLFAGQKLVWSI 339
Cdd:COG0418 328 DTLVPFRAGETLNWRV 343
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
14-339 |
2.24e-119 |
|
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: 347.96 E-value: 2.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEAC-KNDEFEPHVTIFFQVDYSYEFLKEIK 92
Cdd:TIGR00856 9 DWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVpAGHDFTPLMTLYLTDSLTPEELERAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 93 DE--IIAVKLYPFGVTTNSETGVSsmDVEVLRPTLESMEKLGIPLCVHGE-TKG--FMMDREKEFLPIY-ESLAINFPDL 166
Cdd:TIGR00856 89 NEgvVRAVKLYPAGATTNSSHGVT--DIDAIMPVLEAMEKIGLPLLLHGEvTHGdiDIFDREARFIESVlEPLRQRFPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 167 KIMMEHISSKESIDLLKKYDN-LYATITVHHLMLTLDDVVGGMLNPHAFCKPIVKKPEDRKALLQLALSAHPKVMFGSDS 245
Cdd:TIGR00856 167 KVVLEHITTKDAIDYVEDGNNrLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKFFLGTDS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 246 APHQKNTKECHHGAAGVFTSPIALQVLTQLFEEHGKLDNLNAFISLNAQRIYNLNPIKKEIRLIKKDFIVPEVYSYKSEQ 325
Cdd:TIGR00856 247 APHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESIALTDDT 326
|
330
....*....|....
gi 2508954854 326 VVPLFAGQKLVWSI 339
Cdd:TIGR00856 327 LVPFRAGETLSWSV 340
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
14-340 |
2.78e-100 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 300.13 E-value: 2.78e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEAC-KNDEFEPHVTIFFQVDYSYEFLKEIK 92
Cdd:PLN02599 30 DWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALpPGSSFEPLMTLYLTDNTTPEEIKAAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 93 DE--IIAVKLYPFGVTTNSETGVSsmDVEVLRPTLESMEKLGIPLCVHGE-TKGF--MMDREKEFLP-IYESLAINFPDL 166
Cdd:PLN02599 110 ASgvVFAVKLYPAGATTNSQAGVT--DLGKCLPVLEEMAEQGMPLLVHGEvTDPSvdIFDREKVFIDtILAPLVQKLPQL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 167 KIMMEHISSKESIDLLK--KYDNLYATITVHHLMLTLDDVVGGMLNPHAFCKPIVKKPEDRKALLQLALSAHPKVMFGSD 244
Cdd:PLN02599 188 KIVMEHITTMDAVEFVEscGDGNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGSKKFFLGTD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 245 SAPHQKNTKECHHGAAGVFTSPIALQVLTQLFEEHGKLDNLNAFISLNAQRIYNLNPIKKEIRLIKKDFIVPEVYSYKSE 324
Cdd:PLN02599 268 SAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVPEAYSFGGG 347
|
330
....*....|....*.
gi 2508954854 325 QVVPLFAGQKLVWSIS 340
Cdd:PLN02599 348 TVVPMFAGETIPWSVV 363
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
4-300 |
1.03e-19 |
|
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: 89.04 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 4 KNSFIINSALDMHLHLRD------DDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEACKNDefephVTI 77
Cdd:TIGR00857 33 KGLLVLPGFIDLHVHLRDpgeeykEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVD-----VHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 78 FFQVDYSYEfLKEIKDeiiAVKLYPFGVTTN--SETGVSSMDVEVLRPTLESMEKLGIPLCVHGETKGFMM--------- 146
Cdd:TIGR00857 108 YGGVTQGNQ-GKELTE---AYELKEAGAVGRmfTDDGSEVQDILSMRRALEYAAIAGVPIALHAEDPDLIYggvmhegps 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 147 ---------DREKEFLPIyESLAINFPDLK----IMmeHISSKESIDLLKKYDNLYATITV----HHLMLTLDDVVGgmL 209
Cdd:TIGR00857 184 aaqlglparPPEAEEVAV-ARLLELAKHAGcpvhIC--HISTKESLELIVKAKSQGIKITAevtpHHLLLSEEDVAR--L 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 210 NPHAFCKPIVKKPEDRKALLQLALSAHPKVmFGSDSAPHQ-----KNTKECHHGAAGVFTS-PIALQVLTQlfeehgKLD 283
Cdd:TIGR00857 259 DGNGKVNPPLREKEDRLALIEGLKDGIIDI-IATDHAPHTleektKEFAAAPPGIPGLETAlPLLLQLLVK------GLI 331
|
330 340
....*....|....*....|
gi 2508954854 284 NLNAFI---SLNAQRIYNLN 300
Cdd:TIGR00857 332 SLKDLIrmlSINPARIFGLP 351
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
5-315 |
4.97e-18 |
|
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: 83.92 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 5 NSFIINSALDMHLHLRDddmLKLVAPKT--SNTFAGA-------LIMPNLLPPITTKEallAYKKRIQEACKNDEFepHV 75
Cdd:cd01318 1 GLLILPGVIDIHVHFRE---PGLTYKEDfvSGSRAAAaggvttvMDMPNTKPPTTTAE---ALYEKLRLAAAKSVV--DY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 76 TIFFQVDYSYEFLKEIKDEIIAVKLYPfgvttNSETGVSSMDVEVLRPTLESMEKLgipLCVHGETKGFMMDREKEFLPI 155
Cdd:cd01318 73 GLYFGVTGSEDLEELDKAPPAGYKIFM-----GDSTGDLLDDEETLERIFAEGSVL---VTFHAEDEDRLRENRKELKGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 156 YESLAINFPDL-----------------KIMMEHISSKESIDLLKKyDNLYAT--ITVHHLMLTLDDV--VGGMLNphaf 214
Cdd:cd01318 145 SAHPRIRDAEAaavataralklarrhgaRLHICHVSTPEELKLIKK-AKPGVTveVTPHHLFLDVEDYdrLGTLGK---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 215 CKPIVKKPEDRKALLQlALsAHPKV-MFGSDSAPH-----QKNTKECHHGAAGVFTSPIALqvLTQLFEEHGKLDNLNAF 288
Cdd:cd01318 220 VNPPLRSREDRKALLQ-AL-ADGRIdVIASDHAPHtleekRKGYPAAPSGIPGVETALPLM--LTLVNKGILSLSRVVRL 295
|
330 340
....*....|....*....|....*...
gi 2508954854 289 ISLNAQRIYNLnPIKKEIRLIKK-DFIV 315
Cdd:cd01318 296 TSHNPARIFGI-KNKGRIAEGYDaDLTV 322
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
14-301 |
5.90e-14 |
|
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: 71.88 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRD------DDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEA-CKNDEFEPHVTIFFQVdysyE 86
Cdd:cd01317 18 DLHVHLREpgfeykETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVgIVRVLPIGALTKGLKG----E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 87 FLKEIKDEIIAvklypfGVTTNSETGVSSMDVEVLRPTLESMEKLGIPLCVHGETK-----GFMmdREKEF--------- 152
Cdd:cd01317 94 ELTEIGELLEA------GAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPslaggGVM--NEGKVasrlglpgi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 153 LPIYESLAI-------NFPDLKIMMEHISSKESIDLLKKYD----NLYATITVHHLMLTLDDVVGGmlNPHAFCKPIVKK 221
Cdd:cd01317 166 PPEAETIMVardlelaEATGARVHFQHLSTARSLELIRKAKakglPVTAEVTPHHLLLDDEALESY--DTNAKVNPPLRS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 222 PEDRKALLQlALSAHPKVMFGSDSAPHQKNTKECHHGAA--GVFTSPIALQVLTQLFEEHGKLD--NLNAFISLNAQRIY 297
Cdd:cd01317 244 EEDREALIE-ALKDGTIDAIASDHAPHTDEEKDLPFAEAppGIIGLETALPLLWTLLVKGGLLTlpDLIRALSTNPAKIL 322
|
....
gi 2508954854 298 NLNP 301
Cdd:cd01317 323 GLPP 326
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
14-308 |
9.15e-14 |
|
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: 71.27 E-value: 9.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKL---VAPKTSNTFAGALI----MPNLLPP-ITTKEALLAYKKRIQEACKNDEFEPHVTIFFQVDysy 85
Cdd:cd01302 9 DIHVHLRDPGGTTYkedFESGSRAAAAGGVTtvidMPNTGPPpIDLPAIELKIKLAEESSYVDFSFHAGIGPGDVTD--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 86 EFLKEIKDEIIAVKLypFGVTTNSEtGVSSMDVEVLRpTLESMEKLGIPLCVHGETKGFMmdrekeflpiyeslaINFPD 165
Cdd:cd01302 86 ELKKLFDAGINSLKV--FMNYYFGE-LFDVDDGTLMR-TFLEIASRGGPVMVHAERAAQL---------------AEEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 166 LKIMMEHISSKESIDLLKKYDNL----YATITVHHLMLTLDDVvggMLNPHAF-CKPIVKKPEDRKALLQlALSAHPKVM 240
Cdd:cd01302 147 ANVHIAHVSSGEALELIKFAKNKgvkvTCEVCPHHLFLDESML---RLNGAWGkVNPPLRSKEDREALWE-GVKNGKIDT 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2508954854 241 FGSDSAPHQKNTKECHH-------GAAGVFTSpiaLQVLTQLFEEHGKLdnLNAFI---SLNAQRIYNLNPiKKEIRL 308
Cdd:cd01302 223 IASDHAPHSKEEKESGKdiwkappGFPGLETR---LPILLTEGVKRGLS--LETLVeilSENPARIFGLYP-KGTIAV 294
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
14-303 |
1.41e-11 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 64.83 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRD------DDMLklvapktSNTFAGAL-------IMPNLLPPITTKEALLAYKKRIQEACKNDeFEPHVTIFfq 80
Cdd:PRK09357 57 DLHVHLREpgqedkETIE-------TGSRAAAAggfttvvAMPNTKPVIDTPEVVEYVLDRAKEAGLVD-VLPVGAIT-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 81 vdysyeflKEIKDEIIA--VKLYPFGVTTNSETGVSSMDVEVLRPTLESMEKLGIPLCVHGE-----TKGFMMDRE-KEF 152
Cdd:PRK09357 127 --------KGLAGEELTefGALKEAGVVAFSDDGIPVQDARLMRRALEYAKALDLLIAQHCEdpsltEGGVMNEGEvSAR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 153 LPIY------ESLAInFPDLKIMME--------HISSKESIDL---LKKYD-NLYATITVHHLMLTLDDVVGgmLNPHAF 214
Cdd:PRK09357 199 LGLPgipavaEEVMI-ARDVLLAEAtgarvhicHVSTAGSVELirwAKALGiKVTAEVTPHHLLLTDEDLLT--YDPNYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 215 CKPIVKKPEDRKALLQlALSAHPKVMFGSDSAPHQKNTKECHHGAA--GVFTSPIALQVLTQLFEEHGKLDnLNAFI--- 289
Cdd:PRK09357 276 VNPPLRTEEDREALIE-GLKDGTIDAIATDHAPHAREEKECEFEAApfGITGLETALSLLYTTLVKTGLLD-LEQLLekm 353
|
330
....*....|....
gi 2508954854 290 SLNAQRIYNLNPIK 303
Cdd:PRK09357 354 TINPARILGLPAGP 367
|
|
| LigW |
COG2159 |
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ... |
14-301 |
7.29e-11 |
|
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];
Pssm-ID: 441762 [Multi-domain] Cd Length: 253 Bit Score: 61.53 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRD-DDMLKLVAPktsntfAG---ALIMPNLLPPITTKEALLAYKKRIQEACKN--DEFEPHVTIFFQ-VDYSYE 86
Cdd:COG2159 5 DVHTHLGTpEERLADMDE------AGidkAVLSPTPLADPELAALARAANDWLAELVARypDRFIGFATVDPQdPDAAVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 87 FLKEIKDE--IIAVKLYPFgvttnseTGVSSMDVEVLRPTLESMEKLGIPLCVHGETKGFMMDREKEFL---PIYESLAI 161
Cdd:COG2159 79 ELERAVEElgFRGVKLHPA-------VGGFPLDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYaapLILSGVAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 162 NFPDLKIMMEHISS----KESIDLLKKYDNLYATITVHHLmltlddvvggmlnphafckpivkkpedRKALLQLALSAHP 237
Cdd:COG2159 152 RFPDLKFILAHGGGpwlpELLGRLLKRLPNVYFDTSGVFP---------------------------RPEALRELLETLG 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2508954854 238 --KVMFGSDsAPHqkntkechhgaagvFTSPIALQVltqlFEEHGKLDN--LNAFISLNAQRIYNLNP 301
Cdd:COG2159 205 adRILFGSD-YPH--------------WDPPEALEA----LEELPGLSEedREKILGGNAARLLGLDA 253
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
2-262 |
2.61e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 60.94 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 2 KDKNSFIINSALDMHLHLRD--DDMLKLVAPKTSNTFAGALI----MPNLLPPITTKEallAYKKRIQEACKNDefephv 75
Cdd:PRK04250 39 KVKGGIILPGLIDVHVHLRDfeESYKETIESGTKAALHGGITlvfdMPNTKPPIMDEK---TYEKRMRIAEKKS------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 76 tiffQVDYSYEFLKE---IKDEIIAVKLYP--FGVTTNsetGVSSMDVEVLRPTLESMeklgipLCVHGETKGFMM---- 146
Cdd:PRK04250 110 ----YADYALNFLIAgncEKAEEIKADFYKifMGASTG---GIFSENFEVDYACAPGI------VSVHAEDPELIRefpe 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 147 -DREKEFLPIYESLAINFPDLKIM-MEHISSKESIDLLKKYDNLYAT--ITVHHLMLTLDDVvggMLNPHAFCKPIVKKP 222
Cdd:PRK04250 177 rPPEAEVVAIERALEAGKKLKKPLhICHISTKDGLKLILKSNLPWVSfeVTPHHLFLTRKDY---ERNPLLKVYPPLRSE 253
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2508954854 223 EDRKALLQlalSAHPKVMFGSDSAPHQKNTKEchHGAAGV 262
Cdd:PRK04250 254 EDRKALWE---NFSKIPIIASDHAPHTLEDKE--AGAAGI 288
|
|
| Amidohydro_2 |
pfam04909 |
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979. |
14-299 |
3.22e-10 |
|
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
Pssm-ID: 428190 [Multi-domain] Cd Length: 283 Bit Score: 60.24 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTF--AGALIMPNLLP---PITTKEALLAYKKRIQEACK--NDEF------EPHVTIFFq 80
Cdd:pfam04909 2 DAHAHLWPDDERIGFDPGGRLPFmkRRGYDPRDASPedlLALGAALGVARAVVVAASCRgaNNRVaaealaRPGRFLGG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 81 VDYSYEFLKEIKDEIIA---------VKLYPfgvttnSETGVSSMDVEVLRPTLESMEKLGIPLCVHGETKGFMMDREKE 151
Cdd:pfam04909 81 VAVVPLDPEDAAAELERavgeagfrgVRLNP------HPGGDPLLGDRLDRPIYEALEELGLPVDIHTGFGDRPEDTRAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 152 FLPIYESLAINFPDLKIMMEH---------ISSKESIDLLKKYDNLYATITVHHLMLTLDDVVGgmlNPHAFCKPIVKKP 222
Cdd:pfam04909 155 QPLLLAGVARKFPDLKIVLDHgggpwipegLDDPAALALLARRPNVYVKLSGLYRDLYFDAPLA---DRPYLARLLEAFG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2508954854 223 EDRkallqlalsahpkVMFGSDsAPH--QKNTKECHHGAAGVFTSPIALQVLTQLFEEhgkldnlnafislNAQRIYNL 299
Cdd:pfam04909 232 PDR-------------ILFGSD-WPHppLEISPDDGVLLDLPLLLALSDEEREKILGG-------------NAARLYGL 283
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
4-299 |
4.06e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 60.55 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 4 KNSFIINSALDMHLHLRDddmLKL-----VAPKTSNTFAGA--LI--MPNLLPPITTKEALLAYKKRIQEACKNDEFeph 74
Cdd:PRK00369 41 QGTLILPGAIDLHVHLRG---LKLsykedVASGTSEAAYGGvtLVadMPNTIPPLNTPEAITEKLAELEYYSRVDYF--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 75 vtIFFQVDYSYEFLKEIKdeIIAVKLYPfgvttnsetgvssMDVEvLRPTLESMEKLGIPLCVHGETKgfMMDR--EKEF 152
Cdd:PRK00369 115 --VYSGVTKDPEKVDKLP--IAGYKIFP-------------EDLE-REETFRVLLKSRKLKILHPEVP--LALKsnRKLR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 153 LPI-YESLAINF--PDLKIMMEHISSKESIDLLKKydnLYAT--ITVHHLMLTLDDVVGGMLNPhafckPIvKKPEDRKA 227
Cdd:PRK00369 175 RNCwYEIAALYYvkDYQNVHITHASNPRTVRLAKE---LGFTvdITPHHLLVNGEKDCLTKVNP-----PI-RDINERLW 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2508954854 228 LLQLALSAHPKVmfgSDSAPHQKNTKE-----CHHGAAGV-FTSPIAlqvLTQLFEEHGKLDNLNAFISLNAQRIYNL 299
Cdd:PRK00369 246 LLQALSEVDAIA---SDHAPHSSFEKLqpyevCPPGIAALsFTPPFI---YTLVSKGILSIDRAVELISTNPARILGI 317
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
14-315 |
3.23e-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: 57.51 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTFAGAL-IMPNLLPPITTKEALLA----YKKRIQEACKNDEFEPHVTIFF--------- 79
Cdd:pfam01979 8 DAHVHLEMGLLRGIPVPPEFAYEALRLgITTMLKSGTTTVLDMGAttstGIEALLEAAEELPLGLRFLGPGcsldtdgel 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 80 --------QVDYSYEFLKEIKDEIIAVKLYPFGVTTNSETGVSSMdvevlrptLESMEKLGIPLCVH-GETKGFMMDREK 150
Cdd:pfam01979 88 egrkalreKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAA--------LEEAKKYGLPVAIHaLETKGEVEDAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 151 EF-------LPIYESLAINFPD-LKIMMEH---ISSKESIDLLKKYDNlyatITVHHLmltlddvvggmlnphafCKPIV 219
Cdd:pfam01979 160 AFgggiehgTHLEVAESGGLLDiIKLILAHgvhLSPTEANLLAEHLKG----AGVAHC-----------------PFSNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 220 KKPEDRKALLQlALSAHPKVMFGSDSAPhqkntkechHGAAGVFTSPIALQVLTQLFEEHG-KLDNLNAFISLNAQRIYN 298
Cdd:pfam01979 219 KLRSGRIALRK-ALEDGVKVGLGTDGAG---------SGNSLNMLEELRLALELQFDPEGGlSPLEALRMATINPAKALG 288
|
330
....*....|....*...
gi 2508954854 299 LNPIKKEIRLIKK-DFIV 315
Cdd:pfam01979 289 LDDKVGSIEVGKDaDLVV 306
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
14-249 |
4.95e-08 |
|
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: 53.49 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 14 DMHLHLRDDDMLKLVAPKTSNTFA------------------------GALIMPNLLPPITTKEALLAYKKRIQEACKND 69
Cdd:cd01292 3 DTHVHLDGSALRGTRLNLELKEAEelspedlyedtlraleallaggvtTVVDMGSTPPPTTTKAAIEAVAEAARASAGIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 70 EF----EPHVTIFFQVDYSYEFLKEIKDEIIAVKlypFGVTTNSETGVSSMDVEVLRPTLESMEKLGIPLCVH-GETKGF 144
Cdd:cd01292 83 VVlglgIPGVPAAVDEDAEALLLELLRRGLELGA---VGLKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHaGELPDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 145 MMDrekeflpIYESLAINFPDLKIMMEHIS--SKESIDLLKKyDNLYATITVHHLMLTlddvvggmlnphafckpiVKKP 222
Cdd:cd01292 160 TRA-------LEDLVALLRLGGRVVIGHVShlDPELLELLKE-AGVSLEVCPLSNYLL------------------GRDG 213
|
250 260
....*....|....*....|....*..
gi 2508954854 223 EDRKAlLQLALSAHPKVMFGSDSAPHQ 249
Cdd:cd01292 214 EGAEA-LRRLLELGIRVTLGTDGPPHP 239
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
13-335 |
8.37e-07 |
|
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: 50.14 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 13 LDMHLHLRD------DDMLKLVAPKTSNTFAGALIMPNLLPPITTKEALLAYKKRIQEACKndefephvtiffqVDYSY- 85
Cdd:cd01316 9 IDVHVHLREpgathkEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKAR-------------CDYAFs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 86 --------EFLKEIKDEIIAVKLYPFgvttNSETGVSSMDVEVLRPTLESMEKlGIPLCVHGETK--------GFMMDRe 149
Cdd:cd01316 76 igatstnaATVGELASEAVGLKFYLN----ETFSTLILDKITAWASHFNAWPS-TKPIVTHAKSQtlaavlllASLHNR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 150 keflpiyeslainfpdlKIMMEHISSKESIDLLK--KYDNLYAT--ITVHHLMLTLDDVVGGMlNPHAfckPIVKKPEDR 225
Cdd:cd01316 150 -----------------SIHICHVSSKEEINLIRlaKARGLKVTceVSPHHLFLSQDDLPRGQ-YEVR---PFLPTREDQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 226 KALLQLALSAHpkvMFGSDSAPHQ---KNTKECHHGAAGVFTS-PIALQVLtqlfeEHGKL--DNLNAFISLNAQRIYNL 299
Cdd:cd01316 209 EALWENLDYID---CFATDHAPHTlaeKTGNKPPPGFPGVETSlPLLLTAV-----HEGRLtiEDIVDRLHTNPKRIFNL 280
|
330 340 350
....*....|....*....|....*....|....*....
gi 2508954854 300 NPIKK---EIRLiKKDFIVPEVYSYKSEQVVPlFAGQKL 335
Cdd:cd01316 281 PPQSDtyvEVDL-DEEWTIPKNPLQSKKGWTP-FEGKKV 317
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
117-303 |
7.55e-05 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 44.13 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 117 DVEVLRpTLESMEKLGIPLCVHGETKGFMMDREKEFL------PIYESL-------------AINFPDL---KIMMEHIS 174
Cdd:cd01314 161 DEELLD-VLKRAKELGALVMVHAENGDVIAELQKKLLaqgktgPEYHALsrppeveaeatarAIRLAELagaPLYIVHVS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 175 SKESIDLL----KKYDNLYATITVHHLMLTLDDVVGGMLNPHAF-CKPIVKKPEDRKALLQlALSAHPKVMFGSDSAPH- 248
Cdd:cd01314 240 SKEAADEIararKKGLPVYGETCPQYLLLDDSDYWKDWFEGAKYvCSPPLRPKEDQEALWD-GLSSGTLQTVGSDHCPFn 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2508954854 249 --QK-----NTKECHHGAAGVFTSpialqvLTQLFEE---HGKLDnLNAFISL---NAQRIYNLNPIK 303
Cdd:cd01314 319 faQKargkdDFTKIPNGVPGVETR------MPLLWSEgvaKGRIT-LEKFVELtstNPAKIFGLYPRK 379
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
172-299 |
1.03e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 43.76 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 172 HISSKESIDLLKKY-DNLYATITVHHLMLTLDDVVGGmLNPHAFCKPIVKKPEDRKALLQLALSAHPKVMfGSDSAPHQK 250
Cdd:PRK09060 234 HVSTAEEIDFLADHkDVATVEVTPHHLTLAAPECYER-LGTLAQMNPPIRDARHRDGLWRGVRQGVVDVL-GSDHAPHTL 311
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 251 NTKE-----CHHGAAGVftspialQVLTQLFEEH---GKLdNLNAFISL---NAQRIYNL 299
Cdd:PRK09060 312 EEKAkpypaSPSGMTGV-------QTLVPIMLDHvnaGRL-SLERFVDLtsaGPARIFGI 363
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
42-254 |
1.35e-03 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 40.24 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 42 MPNLLPPITTKEALLAYKKRIQEACkndefephvtiffQVDYSYEF------LKEIKD----EIIAVKLYpfgvtTNSET 111
Cdd:PRK09236 92 MPNTNPPTTTLEALEAKYQIAAQRS-------------LANYSFYFgatndnLDEIKRldpkRVCGVKVF-----MGAST 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 112 GvsSMDVEvlRPtlESMEKL----GIPLCVHGETKGFMMDREKEF-------LPI------------YES--LAINFP-- 164
Cdd:PRK09236 154 G--NMLVD--NP--ETLERIfrdaPTLIATHCEDTPTIKANLAKYkekygddIPAemhplirsaeacYKSssLAVSLAkk 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 165 ---DLKIMmeHISSKESIDLLK----KYDNLYATITVHHLMLTLDDVvgGMLNPHAFCKPIVKKPEDRKALLQLALSAHP 237
Cdd:PRK09236 228 hgtRLHVL--HISTAKELSLFEngplAEKRITAEVCVHHLWFDDSDY--ARLGNLIKCNPAIKTASDREALRQALADDRI 303
|
250
....*....|....*..
gi 2508954854 238 KVMfGSDSAPHQKNTKE 254
Cdd:PRK09236 304 DVI-ATDHAPHTWEEKQ 319
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
5-253 |
1.81e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 39.84 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 5 NSFIINSALDMHLHLRD---DDMLKLVAPKTSNTFAGALI---MPNLLPPITTKEAlLAYKKRIQEACKNDEFEPHvtiF 78
Cdd:PRK01211 41 KGAILPAATDIHVHFRTpgeTEKEDFSTGTLSAIFGGTTFimdMPNNNIPIKDYNA-FSDKLGRVAPKAYVDFSLY---S 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 79 FQVDYSYEFLKEIKdeiIAVKLYpFGVTTNSeTGVSSMDVEVlrptlESMEKLGIPLCVHGETKGFMMDREKE------- 151
Cdd:PRK01211 117 METGNNALILDERS---IGLKVY-MGGTTNT-NGTDIEGGEI-----KKINEANIPVFFHAELSECLRKHQFEsknlrdh 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508954854 152 --FLPIY-ESLAINF-PDLKIMMEHISSKESIDllkKYDNLYATITVHHLMLTLDDVVG--GMLNPhafckPIVKKPEDR 225
Cdd:PRK01211 187 dlARPIEcEIKAVKYvKNLDLKTKIIAHVSSID---VIGRFLREVTPHHLLLNDDMPLGsyGKVNP-----PLRDRWTQE 258
|
250 260
....*....|....*....|....*...
gi 2508954854 226 KaLLQLALSAHPKVMfGSDSAPHQKNTK 253
Cdd:PRK01211 259 R-LLEEYISGRFDIL-SSDHAPHTEEDK 284
|
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