|
Name |
Accession |
Description |
Interval |
E-value |
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
3-453 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 766.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNIDVGIARSCDDFFTGTRAA 82
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 83 ACGGTTTIIDhMGFGPNGCRLRHQLEVYRGYAAHKAVIDYSFHGVIQHINHAILDE-IPMIVEEGLSSFKLYLTYQYKL- 160
Cdd:TIGR02033 81 AAGGTTTIID-FVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEhIPEVKEEGINSFKVFMAYKNLLm 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 161 -NDDEVLQALRRLHESGALTTVHPENDAAIASKRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAgNAPLYIVH 239
Cdd:TIGR02033 160 vDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALA-DAPLYVVH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 240 LSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYD--TEDGMKFILSPPLRNVREQDKLWCGISDGAIDVVATDHCTF 317
Cdd:TIGR02033 239 VSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDkpGFEGAKYVCSPPLREPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 318 SMAQRLQISKGDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLWPQKGLLAPGSDGDVVIIDPR 397
Cdd:TIGR02033 319 NFAQKKAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 90111504 398 QSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAGRGRFLRR 453
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-460 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 752.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVNADGQAKQDLLIESGIVRQLGNNIspqlPYEEIDATGCYVFPGGVDVHTHFNIDVGIARSCDDFFTGTR 80
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGANL----GDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 81 AAACGGTTTIIDhMGFGPNGCRLRHQLEVYRGYAAHKAVIDYSFHGVIQHINHAILDEIPMIVEEGLSSFKLYLTYQ--Y 158
Cdd:PRK08323 77 AAACGGTTTIID-FALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEEGITSFKLFMAYKgaL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 159 KLNDDEVLQALRRLHESGALTTVHPENDAAIASKRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAGnAPLYIV 238
Cdd:PRK08323 156 MLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAG-APLYIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 239 HLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDTED---GMKFILSPPLRNVREQDKLWCGISDGAIDVVATDHC 315
Cdd:PRK08323 235 HVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDwfeGAKYVMSPPLRDKEHQDALWRGLQDGDLQVVATDHC 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 316 TFSMAQRLQISKGDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLWPQKGLLAPGSDGDVVIID 395
Cdd:PRK08323 315 PFCFEQKKQLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111504 396 PRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAGRGRFLRRKPFVPPV 460
Cdd:PRK08323 395 PNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQAVV 459
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-448 |
0e+00 |
|
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: 680.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNIDVGIARSCDDFFTGTRAA 82
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 83 ACGGTTTIIDHMGFGPnGCRLRHQLEVYRGYAAHKAVIDYSFHGVIQHINHAILDEIPMIVEEGLSSFKLYLTYQYKL-- 160
Cdd:cd01314 81 AAGGTTTIIDFAIPNK-GQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVKKGISSFKVFMAYKGLLmv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 161 NDDEVLQALRRLHESGALTTVHPENDAAIASKRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAgNAPLYIVHL 240
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELA-GAPLYIVHV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 241 SNGLGLDYLRLARANHQPVWVETCPQYLLLDERSY--DTEDGMKFILSPPLRNVREQDKLWCGISDGAIDVVATDHCTFS 318
Cdd:cd01314 239 SSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYwkDWFEGAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGSDHCPFN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 319 MAQRLQIsKGDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLWPQKGLLAPGSDGDVVIIDPRQ 398
Cdd:cd01314 319 FAQKARG-KDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 90111504 399 SQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAGRG 448
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-453 |
9.06e-173 |
|
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: 491.91 E-value: 9.06e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 4 LIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNIDVGiaRSCDDFFTGTRAAA 83
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 84 CGGTTTIIDHmgfgPN---GCRLRHQLEVYRGYAAHKAVIDYSFHGVIQHINHAILDEIPMIVEEGLSSFKLYLTYQYK- 159
Cdd:COG0044 79 AGGVTTVVDM----PNtnpVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALAEAGAVAFKVFMGSDDGn 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 160 --LNDDEVLQALRRLHESGALTTVHPENDAAIaskRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAGnAPLYI 237
Cdd:COG0044 155 pvLDDGLLRRALEYAAEFGALVAVHAEDPDLI---RGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETG-ARLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 238 VHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDTEDGmKFILSPPLRNVREQDKLWCGISDGAIDVVATDHCTF 317
Cdd:COG0044 231 VHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGT-NFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 318 SMAQRLqiskGDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLwPQKGLLAPGSDGDVVIIDPR 397
Cdd:COG0044 310 TLEEKE----LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPD 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 90111504 398 QSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAgRGRFLRR 453
Cdd:COG0044 385 AEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP-RGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
5-453 |
8.71e-152 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 440.29 E-value: 8.71e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 5 IKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLpyEEIDATGCYVFPGGVDVHTHFNIDVGIA-RSCDDFFTGTRAAA 83
Cdd:PRK13404 8 IRGGTVVTATDTFQADIGIRGGRIAALGEGLGPGA--REIDATGRLVLPGGVDSHCHIDQPSGDGiMMADDFYTGTVSAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 84 CGGTTTIIDhmgFGPN--GCRLRHQLEVYRGYAAHKAVIDYSFHGVIQHINHAIL-DEIPMIVEEGLSSFKLYLTYQ-YK 159
Cdd:PRK13404 86 FGGTTTVIP---FAAQhrGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVLtEELPALIAQGYTSFKVFMTYDdLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 160 LNDDEVLQALRRLHESGALTTVHPENDAAIASKRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAGnAPLYIVH 239
Cdd:PRK13404 163 LDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVD-VPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 240 LSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDTE--DGMKFILSPPLRNVREQDKLWCGISDGAIDVVATDHCTF 317
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDRPgmEGAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 318 smaqRLQISKG--------DFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLWPQKGLLAPGSDG 389
Cdd:PRK13404 322 ----RFDDTDGklaaganpSFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111504 390 DVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAGRGRFLRR 453
Cdd:PRK13404 398 DIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-456 |
1.15e-122 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 366.09 E-value: 1.15e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 2 RVLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNIDVGIARSCDDFFTGTRA 81
Cdd:PLN02942 6 KILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 82 AACGGTTTIIDHMGfgPNGCRLRHQLEVYRGYAAhKAVIDYSFHGVIQHINHAILDEIPMIVEE-GLSSFKLYLTYQYKL 160
Cdd:PLN02942 86 ALAGGTTMHIDFVI--PVNGNLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEkGINSFKFFMAYKGSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 161 --NDDEVLQALRRLHESGALTTVHPENDAAIASKRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAgNAPLYIV 238
Cdd:PLN02942 163 mvTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFV-NTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 239 HLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDTED---GMKFILSPPLRNVREQDKLWCGISDGAIDVVATDHC 315
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDftiASKYVMSPPIRPAGHGKALQAALSSGILQLVGTDHC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 316 TFSMAQRlQISKGDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLWPQKGLLAPGSDGDVVIID 395
Cdd:PLN02942 322 PFNSTQK-AFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111504 396 PRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAGRGRFLRRKPF 456
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPF 461
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
3-452 |
1.72e-92 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 287.36 E-value: 1.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQlPYEEIDATGCYVFPGGVDVHTHFNiDVGiaRS-CDDFFTGTRA 81
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPDILGP-AAKIIDAGGLVVFPGVVDTHVHIN-EPG--RTeWEGFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 82 AACGGTTTIIDhMgfgPNGC--------RLRHQLEVyrgyAAHKAVIDYSFHGVIQHINhaiLDEIPMIVEEGLSSFKLY 153
Cdd:TIGR03178 78 AAAGGITTYID-M---PLNSipatttraSLEAKFEA----AKGKLAVDVGFWGGLVPYN---LDDLRELDEAGVVGFKAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 154 LTYQ-----YKLNDDEVLQALRRLHESGALTTVHPENDAAIASKRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQ 228
Cdd:TIGR03178 147 LSPSgddefPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 229 IAGnAPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDtEDGMKFILSPPLRNVREQDKLWCGISDGAID 308
Cdd:TIGR03178 227 VTG-CRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVP-DGGTLAKCAPPIRDLANQEGLWEALLNGLID 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 309 VVATDH--CTFSMAQrlqisKGDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLwPQKGLLAPG 386
Cdd:TIGR03178 305 CVVSDHspCTPDLKR-----AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPG 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111504 387 SDGDVVIIDPRQS-----QQIQHRHLHdnadySPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAgRGRFLR 452
Cdd:TIGR03178 379 KDADFVFVDPDESytltpDDLYYRHKV-----SPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP-KGQLLL 443
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
3-452 |
1.94e-90 |
|
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: 281.87 E-value: 1.94e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNiDVGiaRS-CDDFFTGTRA 81
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHIN-EPG--RTeWEGFETGTKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 82 AACGGTTTIIDH-MGFGP---NGCRLRHQLEVYRGyaahKAVIDYSFHGVIQHINhaiLDEIPMIVEEGLSSFKLYLT-- 155
Cdd:cd01315 79 AAAGGITTIIDMpLNSIPpttTVENLEAKLEAAQG----KLHVDVGFWGGLVPGN---LDQLRPLDEAGVVGFKCFLCps 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 156 ----YQyKLNDDEVLQALRRLHESGALTTVHPENDAAIASKRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAG 231
Cdd:cd01315 152 gvdeFP-AVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 232 nAPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDerSYDTED-GMKFILSPPLRNVREQDKLWCGISDGAIDVV 310
Cdd:cd01315 231 -CRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFT--AEDVPDgGTEFKCAPPIRDAANQEQLWEALENGDIDMV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 311 ATDH--CTFSMAQrlqISKGDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLWPQKGLLAPGSD 388
Cdd:cd01315 308 VSDHspCTPELKL---LGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYD 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111504 389 GDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAgRGRFLR 452
Cdd:cd01315 385 ADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP-LGQLLL 447
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
49-428 |
3.93e-82 |
|
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: 256.93 E-value: 3.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 49 CYVFPGGVDVHTHFNIDVGIARScDDFFTGTRAAACGGTTTIIDHMGFGPNGCRLRHQLEVYRGYAAhKAVIDYSFHGVI 128
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEE-SSYVDFSFHAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 129 QHINHaiLDEIPMIVEEGLSSFKLYL-TYQYKL---NDDEVLQALRRLHESGALTTVHpendaaiaskraefiaagltap 204
Cdd:cd01302 79 GPGDV--TDELKKLFDAGINSLKVFMnYYFGELfdvDDGTLMRTFLEIASRGGPVMVH---------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 205 ryhalsrpleCEaeaiaRMINLAQIAGnAPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDtEDGMKFI 284
Cdd:cd01302 135 ----------AE-----RAAQLAEEAG-ANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLR-LNGAWGK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 285 LSPPLRNVREQDKLWCGISDGAIDVVATDHCTFSMAQrlQISKGDFSRCPNGLPGVENRMQLLFSSGVMTGRITpERFVE 364
Cdd:cd01302 198 VNPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEE--KESGKDIWKAPPGFPGLETRLPILLTEGVKRGLSL-ETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111504 365 LTSAMPARLFGLWPqKGLLAPGSDGDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRT 428
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
4-454 |
9.59e-82 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 259.58 E-value: 9.59e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 4 LIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNiDVGIARScDDFFTGTRAAA 83
Cdd:PRK02382 5 LLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFR-EPGYTHK-ETWYTGSRSAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 84 CGGTTTIIDHmgfgPN-------GCRLRHQLEVyrgyAAHKAVIDYSFHGVIQhinhAILDEIPMIVEEGLSSF-KLYL- 154
Cdd:PRK02382 83 AGGVTTVVDQ----PNtdpptvdGESFDEKAEL----AARKSIVDFGINGGVT----GNWDPLESLWERGVFALgEIFMa 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 155 --TYQYKLNDDEVLQALRRLHESGALTTVHPEnDAAIASKRAEfIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAGn 232
Cdd:PRK02382 151 dsTGGMGIDEELFEEALAEAARLGVLATVHAE-DEDLFDELAK-LLKGDADADAWSAYRPAAAEAAAVERALEVASETG- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 233 APLYIVHLSNGLGLDYLRLARANhqpvwVETCPQYLLLDERSYDtEDGMKFILSPPLRNVREQDKLWCGISDGAIDVVAT 312
Cdd:PRK02382 228 ARIHIAHISTPEGVDAARREGIT-----CEVTPHHLFLSRRDWE-RLGTFGKMNPPLRSEKRREALWERLNDGTIDVVAS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 313 DHCTFSMAQRlqisKGDFSRCPNGLPGVENRMQLLFsSGVMTGRITPERFVELTSAMPARLFGLwPQKGLLAPGSDGDVV 392
Cdd:PRK02382 302 DHAPHTREEK----DADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLV 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111504 393 IIDPRQSQQIQHRHLHDNADYSPWEGFTcqgAI--VRTLSRGETIFCDGTFTGKAGRGRFLRRK 454
Cdd:PRK02382 376 LVDPDAAREIRGDDLHSKAGWTPFEGME---GVfpELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
3-455 |
2.22e-81 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 258.86 E-value: 2.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQlPYEEIDATGCYVFPGGVDVHTHFNiDVGIARsCDDFFTGTRAA 82
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSP-AREIIDADGLYVFPGMIDVHVHFN-EPGRTH-WEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 83 ACGGTTTIIDhMGFGPNGCRL-RHQLEVYRGYAAHKAVIDYSFHGVIQHINhaiLDEIPMIVEEGLSSFKLYL----TYQ 157
Cdd:PRK06189 82 AAGGCTTYFD-MPLNSIPPTVtREALDAKAELARQKSAVDFALWGGLVPGN---LEHLRELAEAGVIGFKAFMsnsgTDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 158 YKLNDDEVL-QALRRLHESGALTTVHPENDAAIASKRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAGnAPLY 236
Cdd:PRK06189 158 FRSSDDLTLyEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETG-CPLH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 237 IVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERsyDTED-GMKFILSPPLRNVREQDKLWCGISDGAIDVVATDH- 314
Cdd:PRK06189 237 FVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEE--DFERiGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHs 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 315 -CTFSMAQRLqiskgDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLwPQKGLLAPGSDGDVVI 393
Cdd:PRK06189 315 pCPPELKEGD-----DFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADADFVL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111504 394 IDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAgRGRFLRRKP 455
Cdd:PRK06189 389 VDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVFPPP-RGQLLRPSV 449
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
48-432 |
1.13e-63 |
|
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: 209.88 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 48 GCYVFPGGVDVHTHFNiDVGIARScDDFFTGTRAAACGGTTTIIDhMgfgPNGCRLRHQLEVYR---GYAAHKAVIDYSF 124
Cdd:cd01318 1 GLLILPGVIDIHVHFR-EPGLTYK-EDFVSGSRAAAAGGVTTVMD-M---PNTKPPTTTAEALYeklRLAAAKSVVDYGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 125 H-GVIQHINHAILDEIPMIveeglsSFKLYLTYQYK-LNDDEvlQALRRLHESGA-LTTVHPENDAAIASKRAEFIAAGl 201
Cdd:cd01318 75 YfGVTGSEDLEELDKAPPA------GYKIFMGDSTGdLLDDE--ETLERIFAEGSvLVTFHAEDEDRLRENRKELKGES- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 202 taprYHALSRPLECEAEAIARMINLAQIAGnAPLYIVHLSNGlglDYLRLARANHQPVWVETCPQYLLLDERSYDTEDGM 281
Cdd:cd01318 146 ----AHPRIRDAEAAAVATARALKLARRHG-ARLHICHVSTP---EELKLIKKAKPGVTVEVTPHHLFLDVEDYDRLGTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 282 kFILSPPLRNVREQDKLWCGISDGAIDVVATDHCTFSMAQRLQiskgDFSRCPNGLPGVENRMQLLFSSgVMTGRITPER 361
Cdd:cd01318 218 -GKVNPPLRSREDRKALLQALADGRIDVIASDHAPHTLEEKRK----GYPAAPSGIPGVETALPLMLTL-VNKGILSLSR 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111504 362 FVELTSAMPARLFGLwPQKGLLAPGSDGDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRG 432
Cdd:cd01318 292 VVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-451 |
1.54e-63 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 211.84 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVNADGQA-KQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNiDVGIARScDDFFTGT 79
Cdd:PRK07575 3 MSLLIRNARILLPSGELlLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFR-EPGLEHK-EDLFTAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 80 RAAACGGTTTIIDhMgfgPNG-------CRLRHQLEVyrgyAAHKAVIDYSFHgviqhINhAILDEIPMIVEE----GLS 148
Cdd:PRK07575 81 RACAKGGVTSFLE-M---PNTkpltttqAALDDKLAR----AAEKCVVNYGFF-----IG-ATPDNLPELLTAnptcGIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 149 SFKLYLTYQYKLNDDEVLQalRRLHESGALTTVHPENDAAIASKRAEFiaAGLTAPRYHALSRPLECEAEAIARMINLAQ 228
Cdd:PRK07575 147 IFMGSSHGPLLVDEEAALE--RIFAEGTRLIAVHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 229 iAGNAPLYIVHLSNGLGLDYLRlaraNHQPVWV--ETCPQYLLLDERSYDTEdGMKFILSPPLRNVREQDKLWCGISDGA 306
Cdd:PRK07575 223 -KYQRRLHILHLSTAIEAELLR----QDKPSWVtaEVTPQHLLLNTDAYERI-GTLAQMNPPLRSPEDNEALWQALRDGV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 307 IDVVATDHCTFSMAQRLQiskgDFSRCPNGLPGVENRMQLLFSSgVMTGRITPERFVELTSAMPARLFGLwPQKGLLAPG 386
Cdd:PRK07575 297 IDFIATDHAPHTLEEKAQ----PYPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPG 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111504 387 SDGDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAgRGRFL 451
Cdd:PRK07575 371 YDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVNTEV-RGQAL 434
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
20-433 |
3.43e-62 |
|
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: 207.68 E-value: 3.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 20 DLLIESGIVRQLGNNISPqlPYEE-IDATGCYVFPGGVDVHTHFNiDVGIARScDDFFTGTRAAACGGTTTIIDhMgfgP 98
Cdd:TIGR00857 7 DILVEGGRIKKIGKLRIP--PDAEvIDAKGLLVLPGFIDLHVHLR-DPGEEYK-EDIESGSKAAAHGGFTTVAD-M---P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 99 NGCRLRHQLEVYR---GYAAHKAVIDYSFHGVIQHINHA-ILDEIPMIVEEGLSSfKLYLTYQYKLNDDEVLQ-ALRRLH 173
Cdd:TIGR00857 79 NTKPPIDTPETLEwklQRLKKVSLVDVHLYGGVTQGNQGkELTEAYELKEAGAVG-RMFTDDGSEVQDILSMRrALEYAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 174 ESGALTTVHPENDAAIA-SKRAEfiaaGLTAPRYHALSRPLECEAEAIARMINLAQIAGnAPLYIVHLSNGLGLDYLRLA 252
Cdd:TIGR00857 158 IAGVPIALHAEDPDLIYgGVMHE----GPSAAQLGLPARPPEAEEVAVARLLELAKHAG-CPVHICHISTKESLELIVKA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 253 RANHQPVWVETCPQYLLLDERSYDTEDGM-KFilSPPLRNVREQDKLWCGISDGAIDVVATDHCTFSMAQRLQiskgDFS 331
Cdd:TIGR00857 233 KSQGIKITAEVTPHHLLLSEEDVARLDGNgKV--NPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTK----EFA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 332 RCPNGLPGVENRMQLLFSsGVMTGRITPERFVELTSAMPARLFGLwPQKGLLAPGSDGDVVIIDPRQSQQIQHRHLHDNA 411
Cdd:TIGR00857 307 AAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAETFYSKA 384
|
410 420
....*....|....*....|..
gi 90111504 412 DYSPWEGFTCQGAIVRTLSRGE 433
Cdd:TIGR00857 385 KNTPFEGMSLKGKPIATILRGK 406
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
3-452 |
2.34e-54 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 187.82 E-value: 2.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGTVVNADGQAKQDLLIESGIVRQLGNnISPQLPYEEIDATGCYVFPGGVDVHTHFNiDVGIARScDDFFTGTRAA 82
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGD-LSGASAGEVIDCRGLHVLPGVIDSQVHFR-EPGLEHK-EDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 83 ACGGTTTIIDhMgfgPN-------GCRLRHQLEvyrgYAAHKAVIDYSFHGVIQHINHAILDEIPMIveEGLSSFKLYL- 154
Cdd:PRK09060 84 VLGGVTAVFE-M---PNtnpltttAEALADKLA----RARHRMHCDFAFYVGGTRDNADELAELERL--PGCAGIKVFMg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 155 --TYQYKLNDDEVLQA-LRRLHESGAlttVHPENDAAIASKRAEFIAAgltAPRYHALSRPLECEAEAIARMINLAQIAG 231
Cdd:PRK09060 154 ssTGDLLVEDDEGLRRiLRNGRRRAA---FHSEDEYRLRERKGLRVEG---DPSSHPVWRDEEAALLATRRLVRLARETG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 232 nAPLYIVHLSNGLGLDYLRLARANhqpVWVETCPQYLLLD-ERSYDTEdGMKFILSPPLRNVREQDKLWCGISDGAIDVV 310
Cdd:PRK09060 228 -RRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLAaPECYERL-GTLAQMNPPIRDARHRDGLWRGVRQGVVDVL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 311 ATDHCTFSMAQRLQiskgDFSRCPNGLPGVENRMQLLFSSgVMTGRITPERFVELTSAMPARLFGLwPQKGLLAPGSDGD 390
Cdd:PRK09060 303 GSDHAPHTLEEKAK----PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDAD 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111504 391 VVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAgRGRFLR 452
Cdd:PRK09060 377 FTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELVGPP-TGEPVR 437
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
4-451 |
1.72e-53 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 185.44 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 4 LIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPqlPYEEIDATGCYVFPGGVDVHTHFNiDVGiARSCDDFFTGTRAAA 83
Cdd:PRK08044 6 IIKNGTVILENEARVVDIAVKGGKIAAIGQDLGD--AKEVMDASGLVVSPGMVDAHTHIS-EPG-RSHWEGYETGTRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 84 CGGTTTIIDhMGFGPNGCRL-RHQLEVYRGYAAHKAVIDYSFHGVIQHINhaiLDEIPMIVEEGLSSFKLYLT------- 155
Cdd:PRK08044 82 KGGITTMIE-MPLNQLPATVdRASIELKFDAAKGKLTIDAAQLGGLVSYN---LDRLHELDEVGVVGFKCFVAtcgdrgi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 156 ---YQyKLNDDEVLQALRRLHESGALTTVHPENdAAIASKRAEfIAA--GLTAPRYHALSRPLECEAEAIARMINLAQIA 230
Cdd:PRK08044 158 dndFR-DVNDWQFYKGAQKLGELGQPVLVHCEN-ALICDELGE-EAKreGRVTAHDYVASRPVFTEVEAIRRVLYLAKVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 231 GnAPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDtEDGMKFILSPPLRNVREQDKLWCGISDGAIDVV 310
Cdd:PRK08044 235 G-CRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFE-EIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 311 ATDH--CTFSMaqrlqiSKGDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLwPQKGLLAPGSD 388
Cdd:PRK08044 313 VSDHspCPPEM------KAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKD 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111504 389 GDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAGRGRFL 451
Cdd:PRK08044 386 ADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFI 448
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
42-428 |
2.32e-51 |
|
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: 177.81 E-value: 2.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 42 EEIDATGCYVFPGGVDVHTHFNIDVGIARscDDFFTGTRAAACGGTTTIIdhmgFGPNGCRLRHQLEVYRGYA--AHKAv 119
Cdd:cd01317 3 EVIDAEGKILAPGLVDLHVHLREPGFEYK--ETLESGAKAAAAGGFTTVV----CMPNTNPVIDNPAVVELLKnrAKDV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 120 iDYSFHGVIQHI----NHAILDEIPMIVEEGLSSF----KLYLtyqyklnDDEVLQ-ALRRLHESGALTTVHPE------ 184
Cdd:cd01317 76 -GIVRVLPIGALtkglKGEELTEIGELLEAGAVGFsddgKPIQ-------DAELLRrALEYAAMLDLPIIVHPEdpslag 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 185 ----NDAAIASKraefiaAGLTapryhalSRPLECEAEAIARMINLAQIAGnAPLYIVHLSNGLGLDYLRLARANHQPVW 260
Cdd:cd01317 148 ggvmNEGKVASR------LGLP-------GIPPEAETIMVARDLELAEATG-ARVHFQHLSTARSLELIRKAKAKGLPVT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 261 VETCPQYLLLDE---RSYDTedgmKFILSPPLRNVREQDKLWCGISDGAIDVVATDHCTFSMAQRLQiskgDFSRCPNGL 337
Cdd:cd01317 214 AEVTPHHLLLDDealESYDT----NAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDL----PFAEAPPGI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 338 PGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLWPqkGLLAPGSDGDVVIIDPRQSQQIQHRHLHDNADYSPWE 417
Cdd:cd01317 286 IGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFD 363
|
410
....*....|.
gi 90111504 418 GFTCQGAIVRT 428
Cdd:cd01317 364 GQKLKGRVLAT 374
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-433 |
3.61e-51 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 178.85 E-value: 3.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVNADGQ-AKQDLLIESGIVRQLGNNISPQLPyEEIDATGCYVFPGGVDVHTHFNiDVGIARScDDFFTGT 79
Cdd:PRK09357 1 MMILIKNGRVIDPKGLdEVADVLIDDGKIAAIGENIEAEGA-EVIDATGLVVAPGLVDLHVHLR-EPGQEDK-ETIETGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 80 RAAACGGTTTIIdHMgfgPNGcrlrhqlevyrgyaahKAVIDySFHGVIQHINHAilDEIPMI-VE-----------EGL 147
Cdd:PRK09357 78 RAAAAGGFTTVV-AM---PNT----------------KPVID-TPEVVEYVLDRA--KEAGLVdVLpvgaitkglagEEL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 148 SSFKLYLTYQYK-LNDD--EVLQA--LRR-LHESGALTTV---HPEnDAAIASKRAefIAAGLTAPRYHALSRPLECEAE 218
Cdd:PRK09357 135 TEFGALKEAGVVaFSDDgiPVQDArlMRRaLEYAKALDLLiaqHCE-DPSLTEGGV--MNEGEVSARLGLPGIPAVAEEV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 219 AIARMINLAQIAGnAPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDTEDGMkFILSPPLRNVREQDKL 298
Cdd:PRK09357 212 MIARDVLLAEATG-ARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPN-YKVNPPLRTEEDREAL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 299 WCGISDGAIDVVATDHCTFSMAQRLQiskgDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLWP 378
Cdd:PRK09357 290 IEGLKDGTIDAIATDHAPHAREEKEC----EFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPA 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 90111504 379 qkGLLAPGSDGDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGE 433
Cdd:PRK09357 366 --GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGK 418
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-452 |
2.11e-47 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 169.28 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNiDVGIARScDDFFTGTR 80
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFR-EPGLTHK-GDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 81 AAACGGTTTIIDHMGFGPNGCRLRhQLEVYRGYAAHKAVIDYSFHGVIQHINhaiLDEIPMIVEEGLSSFKLYL---TYQ 157
Cdd:PRK09236 80 AAVAGGITSFMEMPNTNPPTTTLE-ALEAKYQIAAQRSLANYSFYFGATNDN---LDEIKRLDPKRVCGVKVFMgasTGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 158 YKLNDDEVLQALRRlhESGALTTVHPENDAAIASKRAEFIAA-GLTAP-RYHALSRPLECEAEAIARMINLAQIAGnAPL 235
Cdd:PRK09236 156 MLVDNPETLERIFR--DAPTLIATHCEDTPTIKANLAKYKEKyGDDIPaEMHPLIRSAEACYKSSSLAVSLAKKHG-TRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 236 YIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDTEdGMKFILSPPLRNVREQDKLWCGISDGAIDVVATDHC 315
Cdd:PRK09236 233 HVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARL-GNLIKCNPAIKTASDREALRQALADDRIDVIATDHA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 316 TFSMAQRlqisKGDFSRCPNGLPGVENRMQLLFSSgVMTGRITPERFVELTSAMPARLFGLwPQKGLLAPGSDGDVVIID 395
Cdd:PRK09236 312 PHTWEEK----QGPYFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAILFDI-KERGFIREGYWADLVLVD 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111504 396 PRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTG--KAGRGRFLR 452
Cdd:PRK09236 386 LNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLVEscRGQRLEFDR 444
|
|
| PLN02795 |
PLN02795 |
allantoinase |
51-439 |
2.32e-47 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 170.34 E-value: 2.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 51 VFPGGVDVHTHFNiDVGiaRS-CDDFFTGTRAAACGGTTTIIDhMGFG--PNGCRLRHqLEVYRGYAAHKAVIDYSFHGV 127
Cdd:PLN02795 97 VMPGLIDVHVHLN-EPG--RTeWEGFPTGTKAAAAGGITTLVD-MPLNsfPSTTSVET-LELKIEAAKGKLYVDVGFWGG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 128 I----QHiNHAILDEIpmiVEEGLSSFKLYLTyQYKLND------DEVLQALRRLHESGALTTVHPENDAAIASKraEFI 197
Cdd:PLN02795 172 LvpenAH-NASVLEEL---LDAGALGLKSFMC-PSGINDfpmttaTHIKAALPVLAKYGRPLLVHAEVVSPVESD--SRL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 198 AAGLTAPRYHALSRPLECEAEAIARMINLAQ------IAGNAPLYIVHLSNGLG-LDYLRLARANHQPVWVETCPQYLLL 270
Cdd:PLN02795 245 DADPRSYSTYLKSRPPSWEQEAIRQLLEVAKdtrpggVAEGAHVHIVHLSDAESsLELIKEAKAKGDSVTVETCPHYLAF 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 271 DerSYDTEDG-MKFILSPPLRNVREQDKLWCGISDGAIDVVATDHCTFSMAQRLqISKGDFSRCPNGLPGVENRMQLLFS 349
Cdd:PLN02795 325 S--AEEIPDGdTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKL-LEEGNFLRAWGGISSLQFVLPATWT 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 350 SGVMTGrITPERFVELTSAMPARLFGLwPQKGLLAPGSDGDVVIIDPRQSQQIQHRH--LHDNADYSPWEGFTCQGAIVR 427
Cdd:PLN02795 402 AGRAYG-LTLEQLARWWSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAEFVLDESYpiYHKHKSLSPYLGTKLSGKVIA 479
|
410
....*....|..
gi 90111504 428 TLSRGETIFCDG 439
Cdd:PLN02795 480 TFVRGNLVFLEG 491
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
23-419 |
7.66e-34 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 131.52 E-value: 7.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 23 IESGIVRQLGNNIsPQLPYEEIDATgcyVFPGGVDVHTHFNiDVGIARScDDFFTGTRAAACGGTTTIIDHmgfgPNGcr 102
Cdd:PRK01211 20 VEDGKIKSIKKDA-GNIGKKELKGA---ILPAATDIHVHFR-TPGETEK-EDFSTGTLSAIFGGTTFIMDM----PNN-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 103 lRHQLEVYRGYA------AHKAVIDYSFHGVIQHINHAILDEIPMiveeglsSFKLYLTYQYKLNDDEVL-QALRRLHES 175
Cdd:PRK01211 88 -NIPIKDYNAFSdklgrvAPKAYVDFSLYSMETGNNALILDERSI-------GLKVYMGGTTNTNGTDIEgGEIKKINEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 176 GALTTVHPENDAAIasKRAEFIAAGLtapRYHALSRPLECEAEAIARMINLaqiaGNAPLYIVHLSN-GLGLDYLRlara 254
Cdd:PRK01211 160 NIPVFFHAELSECL--RKHQFESKNL---RDHDLARPIECEIKAVKYVKNL----DLKTKIIAHVSSiDVIGRFLR---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 255 nhqpvwvETCPQYLLLDErsyDTEDGMKFILSPPLRNVREQDKLWCGISDGAIDVVATDHctfsmAQRLQISKGDFSRCP 334
Cdd:PRK01211 227 -------EVTPHHLLLND---DMPLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDH-----APHTEEDKQEFEYAK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 335 NGLPGVENRMQlLFSSGVMTGRITPERFVELTSAMPARLFGLwpQKGLLAPGSDGDVVIIDPRQSQQIQHRHLHDNADYS 414
Cdd:PRK01211 292 SGIIGVETRVP-LFLALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVS 368
|
....*
gi 90111504 415 PWEGF 419
Cdd:PRK01211 369 PFNGF 373
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
21-449 |
4.20e-32 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 126.42 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 21 LLIESGIVRQLGNNispQLPYEE-IDATGCYVFPGGVDVHTHFNidvgiarscdDFF--------TGTRAAACGGTTTII 91
Cdd:PRK04250 17 IGIENGRISKISLR---DLKGKEvIKVKGGIILPGLIDVHVHLR----------DFEesyketieSGTKAALHGGITLVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 92 DHmgfgPNGCRLRHQLEVYR---GYAAHKAVIDYSFhGVIQHINHAILDEIPMIVEE---GLSSFKLYLtyqyklNDDEV 165
Cdd:PRK04250 84 DM----PNTKPPIMDEKTYEkrmRIAEKKSYADYAL-NFLIAGNCEKAEEIKADFYKifmGASTGGIFS------ENFEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 166 LQAlrrlhESGALTTVHPEnDAAIASKRAEfiaagltapryhalsRPLECEAEAIARMINLAQiAGNAPLYIVHLSNGLG 245
Cdd:PRK04250 153 DYA-----CAPGIVSVHAE-DPELIREFPE---------------RPPEAEVVAIERALEAGK-KLKKPLHICHISTKDG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 246 LDylRLARANHQPVWVETCPQYLLLDERSYdtEDGMKFILSPPLRNVREQDKLWCGISDgaIDVVATDHCTFSMAqrlqi 325
Cdd:PRK04250 211 LK--LILKSNLPWVSFEVTPHHLFLTRKDY--ERNPLLKVYPPLRSEEDRKALWENFSK--IPIIASDHAPHTLE----- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 326 skgDFSRCPNGLPGVENRMQLLFSSgVMTGRITPERFVELTSAMPARLFGLwPQKGLlAPGSDGDVVIIDPRQSQQIQHR 405
Cdd:PRK04250 280 ---DKEAGAAGIPGLETEVPLLLDA-ANKGMISLFDIVEKMHDNPARIFGI-KNYGI-EEGNYANFAVFDMKKEWTIKAE 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 90111504 406 HLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKaGRGR 449
Cdd:PRK04250 354 ELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGK-PRGV 396
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
28-454 |
4.61e-29 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 117.55 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 28 VRQLGNNISPQLPYEEidatGCYVFPGGVDVHTHFNidvGIARSC-DDFFTGTRAAACGGTTTIIDhMgfgPNGC----- 101
Cdd:PRK00369 26 IKEIKSRCKPDLDLPQ----GTLILPGAIDLHVHLR---GLKLSYkEDVASGTSEAAYGGVTLVAD-M---PNTIpplnt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 102 --RLRHQLEVYRGYAAhkavIDYS-FHGVIqhinhailDEIPMIVEEGLSSFKLYLtyqyklNDDEVLQALRRLHESGAL 178
Cdd:PRK00369 95 peAITEKLAELEYYSR----VDYFvYSGVT--------KDPEKVDKLPIAGYKIFP------EDLEREETFRVLLKSRKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 179 TTVHPENDAAIASKRAefiaagltapryhaLSRPleCEAEAIArminLAQIAGNAPLYIVHLSNglgLDYLRLARAnhQP 258
Cdd:PRK00369 157 KILHPEVPLALKSNRK--------------LRRN--CWYEIAA----LYYVKDYQNVHITHASN---PRTVRLAKE--LG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 259 VWVETCPQYLLldersYDTEDGMKFILSPPLRNVREQDKLWCGISDgaIDVVATDHCTFSMAQRLQiskgDFSRCPNGLP 338
Cdd:PRK00369 212 FTVDITPHHLL-----VNGEKDCLTKVNPPIRDINERLWLLQALSE--VDAIASDHAPHSSFEKLQ----PYEVCPPGIA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 339 GVENRMQLLFSSgVMTGRITPERFVELTSAMPARLFGLwpQKGLLAPGSDGDVVIIdprQSQQIQHRHLHDNADYSPWEG 418
Cdd:PRK00369 281 ALSFTPPFIYTL-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVI---QFEDWRYSTKYSKVIETPLDG 354
|
410 420 430
....*....|....*....|....*....|....*.
gi 90111504 419 FTCQGAIVRTLSRGETIFCDGTFTGKAGRGRFLRRK 454
Cdd:PRK00369 355 FELKASVYATIVQGKLAYLEGEVFPVKGINPFGERK 390
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
53-448 |
7.44e-23 |
|
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: 99.06 E-value: 7.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 53 PGGVDVHTHFNiDVGIARScDDFFTGTRAAACGGTTTIidhmGFGPNGCRL---RHQLEVYRGYAAHKAVIDYSFHGVIQ 129
Cdd:cd01316 6 PGLIDVHVHLR-EPGATHK-EDFASGTKAALAGGFTMV----RAMPNTNPSivdVASLKLVQSLAQAKARCDYAFSIGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 130 HINHAILDEIP-------MIVEEGLSSFKLyltyqyklndDEVLQALRRLhesgaltTVHPENdaaiaskraefiaaglt 202
Cdd:cd01316 80 STNAATVGELAseavglkFYLNETFSTLIL----------DKITAWASHF-------NAWPST----------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 203 apryhalsRPLECEAEA--IARMINLAQIAgNAPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERsyDTEDG 280
Cdd:cd01316 126 --------KPIVTHAKSqtLAAVLLLASLH-NRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQD--DLPRG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 281 MkFILSPPLRNVREQDKLWCGISdgAIDVVATDHCTFSMAQRlqisKGdfSRCPNGLPGVENRMQLLFSSgVMTGRITPE 360
Cdd:cd01316 195 Q-YEVRPFLPTREDQEALWENLD--YIDCFATDHAPHTLAEK----TG--NKPPPGFPGVETSLPLLLTA-VHEGRLTIE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 361 RFVELTSAMPARLFGLWPQkgllapgsDGDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGT 440
Cdd:cd01316 265 DIVDRLHTNPKRIFNLPPQ--------SDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGE 336
|
....*...
gi 90111504 441 FTGKAGRG 448
Cdd:cd01316 337 IVAPPGFG 344
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
1-436 |
8.43e-22 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 97.05 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVN-ADG-QAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFnidvgiaRSCDDFFTG 78
Cdd:PRK07627 1 MKIHIKGGRLIDpAAGtDRQADLYVAAGKIAAIGQAPAGFNADKTIDASGLIVCPGLVDLSARL-------REPGYEYKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 79 T-----RAAACGGTTTI---------IDHMGfgpngcrlRHQLEVYRGYAAHKAVIdYSFHGVIQHINHAILDEIPMIVE 144
Cdd:PRK07627 74 TlesemAAAVAGGVTSLvcppdtdpvLDEPG--------LVEMLKFRARNLNQAHV-YPLGALTVGLKGEVLTEMVELTE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 145 EGLSSFKlyltyQYK--LNDDEVL-QALRRLHESGALTTVHPEnDAAIAskRAEFIAAGLTAPRYHALSRPLECEAEAIA 221
Cdd:PRK07627 145 AGCVGFS-----QANvpVVDTQVLlRALQYASTFGFTVWLRPL-DAFLG--RGGVAASGAVASRLGLSGVPVAAETIALH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 222 RMINLAQIAGnAPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDTEDGmKFILSPPLRNVREQDKLWCG 301
Cdd:PRK07627 217 TIFELMRVTG-ARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDS-QFRLDPPLRSQRDREAIRAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 302 ISDGAIDVVATDHCTFSMAQRLQiskgDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAmPARLFGLwpQKG 381
Cdd:PRK07627 295 LADGTIDAICSDHTPVDDDEKLL----PFAEATPGATGLELLLPLTLKWADEAKVPLARALARITSA-PARVLGL--PAG 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 90111504 382 LLAPGSDGDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIF 436
Cdd:PRK07627 368 RLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAF 422
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
200-428 |
4.85e-21 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 94.67 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 200 GLTAPRYHALSRPLECEAEAIARMINLAQiAGNAPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDER---SYD 276
Cdd:PRK07369 196 GLLALRLGLPGDPASAETTALAALLELVA-AIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEalaSYD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 277 TEdgmkFILSPPLRNVREQDKLWCGISDGAIDVVATDHCTFSMAQRLQiskgDFSRCPNGLPGVENRMQLLFSSGVMTGR 356
Cdd:PRK07369 275 PN----LRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTV----AFAEAPPGAIGLELALPLLWQNLVETGE 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111504 357 ITPERFVELTSAMPARLFGLWPQKglLAPGSDGDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRT 428
Cdd:PRK07369 347 LSALQLWQALSTNPARCLGQEPPS--LAPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRVLQT 416
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
21-435 |
3.00e-19 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 88.99 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 21 LLIESGIVRQLGNNISPqlpyEEI-DATGCYVFPGGVDVhthfNIdvgiaRSCDDFFTG----TRAAAC--GGTTTII-- 91
Cdd:PRK08417 1 IRIKDGKITEIGSDLKG----EEIlDAKGKTLLPALVDL----NV-----SLKNDSLSSknlkSLENEClkGGVGSIVly 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 92 -DHMGFGPNGcrlrhqlevyrgyaahkAVIDYsfhgvIQHINHaildEIPMIVEEGLSSFKlyltyqyklnDDEVLQALR 170
Cdd:PRK08417 68 pDSTPAIDNE-----------------IALEL-----INSAQR----ELPMQIFPSIRALD----------EDGKLSNIA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 171 RLHESGAL-----TTVHPENDAAIAS-------------KRAEFIAAGL-----TAPRYHALSRPLECEAEAIARMINLA 227
Cdd:PRK08417 112 TLLKKGAKalelsSDLDANLLKVIAQyakmldvpifcrcEDSSFDDSGVmndgeLSFELGLPGIPSIAETKEVAKMKELA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 228 QIAGNaPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERS---YDTedGMKfiLSPPLRNVREQDKLWCGISD 304
Cdd:PRK08417 192 KFYKN-KVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSAcenFNT--AAK--LNPPLRSKEDRLALLEALKE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 305 GAIDVVATDHCTFSmaqrlqISKGD--FSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLwpQKGL 382
Cdd:PRK08417 267 GKIDFLTSLHSAKS------NSKKDlaFDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGE 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 90111504 383 LAPGSDGDVVIIDPRQSQQIQhrhlhDNadYSPWEGFTCQGAIVRTLSRGETI 435
Cdd:PRK08417 339 IEVGKEADLVLFDPNESTIID-----DN--FSLYSGDELYGKIEAVIIKGKLY 384
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
3-447 |
2.42e-18 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 86.58 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGTVVNADGQA--KQDLLIESGIVRQLGNNISPQLPyEEIDATGCYVFPGGVDVHTHFniDVGIARSCDDfftgTR 80
Cdd:cd01297 2 LVIRNGTVVDGTGAPpfTADVGIRDGRIAAIGPILSTSAR-EVIDAAGLVVAPGFIDVHTHY--DGQVFWDPDL----RP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 81 AAACGGTTTIIDHMGFGPNGCRLRHQ---LEVYRGYAAHKAVIDYSFHGVIQHInhAILDEIPMIVEEGLSSFKLYL-TY 156
Cdd:cd01297 75 SSRQGVTTVVLGNCGVSPAPANPDDLarlIMLMEGLVALGEGLPWGWATFAEYL--DALEARPPAVNVAALVGHAALrRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 157 QYKLND----DEVLQALRRLH----ESGAL---TTVHPeNDAAIAsKRAEFIA-AGL---------TAPRYHALSRplec 215
Cdd:cd01297 153 VMGLDAreatEEELAKMRELLrealEAGALgisTGLAY-APRLYA-GTAELVAlARVaaryggvyqTHVRYEGDSI---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 216 eAEAIARMINLAQIAGnAPLYIVHLSN---------GLGLDYLRLARANHQPVWVETCPqyllldeRSYDTEDGMKFILS 286
Cdd:cd01297 227 -LEALDELLRLGRETG-RPVHISHLKSagapnwgkiDRLLALIEAARAEGLQVTADVYP-------YGAGSEDDVRRIMA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 287 PPLRNvreqdklwcGISDG-AIDvvaTDHCTfsmaqrlqiSKGDFSRcpnglpgvenrmqLLFSSGVMTGRITPERFVEL 365
Cdd:cd01297 298 HPVVM---------GGSDGgALG---KPHPR---------SYGDFTR-------------VLGHYVRERKLLSLEEAVRK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 366 TSAMPARLFGLwPQKGLLAPGSDGDVVIIDPrqsqqiqhRHLHDNADY----SPWEGftcqgaIVRTLSRGETIFCDGTF 441
Cdd:cd01297 344 MTGLPARVFGL-ADRGRIAPGYRADIVVFDP--------DTLADRATFtrpnQPAEG------IEAVLVNGVPVVRDGAF 408
|
....*..
gi 90111504 442 TG-KAGR 447
Cdd:cd01297 409 TGaRPGR 415
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
20-436 |
8.56e-18 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 85.09 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 20 DLLIESGIVRQLGNNISPQ-LP--YEEIDATGCYVFPGGVDVHTHfnidVGI--ARSCDDFFTGTRAAACGGTTTI---- 90
Cdd:PRK09059 24 TVLIEDGVIVAAGKGAGNQgAPegAEIVDCAGKAVAPGLVDARVF----VGEpgAEHRETIASASRAAAAGGVTSIimmp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 91 -----IDHMGFgpngcrlrhqLEVYRGYAAHKAVID-YSFHGVIQHINHAILDEIPMIVEEGLSSFklylTYQYK-LNDD 163
Cdd:PRK09059 100 dtdpvIDDVAL----------VEFVKRTARDTAIVNiHPAAAITKGLAGEEMTEFGLLRAAGAVAF----TDGRRsVANT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 164 EVLQ-ALRRLHESGALTTVHPE----------NDAAIAS--------KRAEFIA-------AGLTAPRYHA--LSRPLEC 215
Cdd:PRK09059 166 QVMRrALTYARDFDAVIVHETRdpdlggngvmNEGLFASwlglsgipREAEVIPlerdlrlAALTRGRYHAaqISCAESA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 216 EAEAIARMINLAQIAGnapLYIVHLS---NGLGldylrlaranhqpvwvetcpQYllldeRSYdtedgmkFILSPPLRNv 292
Cdd:PRK09059 246 EALRRAKDRGLKVTAG---VSINHLSlneNDIG--------------------EY-----RTF-------FKLSPPLRT- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 293 rEQDK--LWCGISDGAIDVVATDHctfsMAQRLQISKGDFSRCPNGLPGVENrmqlLFSSG---VMTGRITPERFVELTS 367
Cdd:PRK09059 290 -EDDRvaMVEAVASGTIDIIVSSH----DPQDVDTKRLPFSEAAAGAIGLET----LLAAAlrlYHNGEVPLLRLIEALS 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111504 368 AMPARLFGLwpQKGLLAPGSDGDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIF 436
Cdd:PRK09059 361 TRPAEIFGL--PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVY 427
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
50-435 |
2.86e-16 |
|
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: 79.47 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 50 YVFPGGVDVHTHFNIDVGIARSCDDFF------TGTRAAACGGTTTIIDhMGFGPNGCRLRhQLEvyrgyAAHKAVIDYS 123
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLD-MGATTSTGIEA-LLE-----AAEELPLGLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 124 FHGVIQHINHAILDEIPMIVEEGLSSFKLYLtyqyKLNDDEVLQALRRLHESGALTtvhpENDAAIASKRAEFIAAGLTA 203
Cdd:pfam01979 74 FLGPGCSLDTDGELEGRKALREKLKAGAEFI----KGMADGVVFVGLAPHGAPTFS----DDELKAALEEAKKYGLPVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 204 pryHALSRPLECEA--EAIARMINLAQIAGNAPLYIVhlsnglgLDYLRLARANHQPVWVETcpqYLLLDERSYdtEDGM 281
Cdd:pfam01979 146 ---HALETKGEVEDaiAAFGGGIEHGTHLEVAESGGL-------LDIIKLILAHGVHLSPTE---ANLLAEHLK--GAGV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 282 KFILSPPLRNVREQDKLWCGISDGAIDVVATDHC----TFSMAQRLqiskgdfsrcpnglpgvenRMQLLFSSGVMTGrI 357
Cdd:pfam01979 211 AHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAgsgnSLNMLEEL-------------------RLALELQFDPEGG-L 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111504 358 TPERFVELTSAMPARLFGLWPQKGLLAPGSDGDVVIIDPRQsqqiqhrhlhdnadYSPWEGFTCQGAIVRTLSRGETI 435
Cdd:pfam01979 271 SPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDP--------------LAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-395 |
5.48e-14 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 73.07 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 2 RVLIKNGTVVNADGQA---KQDLLIESGIVRQLGNNISPQLP--YEEIDATGCYVFPGGVDVHTH----------FNIDV 66
Cdd:COG1228 9 TLLITNATLVDGTGGGvieNGTVLVEDGKIAAVGPAADLAVPagAEVIDATGKTVLPGLIDAHTHlglgggraveFEAGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 67 GIARSCDDFFTGTRAAA---CGGTTTIIDHMGfGPNGCR---LRHQLEVYRG---YAAHKAVidYSFHGVIQHINHAILD 137
Cdd:COG1228 89 GITPTVDLVNPADKRLRralAAGVTTVRDLPG-GPLGLRdaiIAGESKLLPGprvLAAGPAL--SLTGGAHARGPEEARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 138 EIPMIVEEGLSSFKLYLTYQYK-LNDDEVLQALRRLHESGALTTVHPENDAAIasKRAefIAAGLTApryhalsrplece 216
Cdd:COG1228 166 ALRELLAEGADYIKVFAEGGAPdFSLEELRAILEAAHALGLPVAAHAHQADDI--RLA--VEAGVDS------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 217 aeaiarminlaqiagnaplyIVHLsNGLGLDYLRLArANHQPVWVetCPQ----YLLLDERSYDTEDGMKFILSPPLRNV 292
Cdd:COG1228 229 --------------------IEHG-TYLDDEVADLL-AEAGTVVL--VPTlslfLALLEGAAAPVAAKARKVREAALANA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 293 REqdklwcgisdgAID-----VVATDHCTFSMaqrlqiskgdfsrcpnglPGVENRMQLlfssGVMT-GRITPERFVELT 366
Cdd:COG1228 285 RR-----------LHDagvpvALGTDAGVGVP------------------PGRSLHREL----ALAVeAGLTPEEALRAA 331
|
410 420
....*....|....*....|....*....
gi 90111504 367 SAMPARLFGLWPQKGLLAPGSDGDVVIID 395
Cdd:COG1228 332 TINAAKALGLDDDVGSLEPGKLADLVLLD 360
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
3-92 |
7.79e-11 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 63.65 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGTVVNADG--QAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNIDVGIarscddffTGTR 80
Cdd:COG3964 2 LLIKGGRVIDPANgiDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHVFPGGTD--------YGVD 73
|
90
....*....|....*
gi 90111504 81 AAACG---GTTTIID 92
Cdd:COG3964 74 PDGVGvrsGVTTVVD 88
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
1-61 |
1.31e-09 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 60.21 E-value: 1.31e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111504 1 MRVLIKNGTVV----NADGQaKQDLLIESG-IVRQLgnniSPQLPYEEIDATGCYVFPGGVDVHTH 61
Cdd:COG1229 1 MELIIKNGRVYdpanGIDGE-VMDIAIKDGkIVEEP----SDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
1-455 |
1.31e-09 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 60.19 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVNADGQA--KQDLLIESGIVRQLGNNISPQLPyEEIDATGCYVFPGGVDVHTHFNIDVGIARSCDdfftg 78
Cdd:COG3653 2 FDLLIRGGTVVDGTGAPpfRADVAIKGGRIVAVGDLAAAEAA-RVIDATGLVVAPGFIDIHTHYDLQLLWDPRLE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 79 trAAACGGTTTII---DHMGFGPNGCRLRHQL-EVYRGYAAHKAVIDYSFHG----------------VIQHINHAIL-- 136
Cdd:COG3653 76 --PSLRQGVTTVVmgnCGVSFAPVRPEDRDRLiDLMEGVEGIPEGLDWDWESfgeyldalerrglgvnVASLVGHGTLra 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 137 ------DEIP-------M--IVEE-------GLSSFKLYL--TYQyklNDDEVLQALRRLHESGALTTVHPENDAAIASK 192
Cdd:COG3653 154 yvmgldDRPPtpeelarMraLLREameagalGLSTGLIYVpgTYA---STDELVALAKVVAEYGGVYQSHMRDEGDGLLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 193 R-AEFIAAGLTAPR----YH--ALSRPLECEAEAIARMINLAQIAGnAPLYIVHLS---NGLGLDYLRlaranhqPVWVE 262
Cdd:COG3653 231 AvDELIRIGREAGVpvhiSHlkAAGKPNWGKADEVLALIEAARAEG-LDVTADVYPypaGSTGLGALL-------PPWAA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 263 TCP---QYLLLDERSY------DTEDGMKFIL-------------SPPL-----RNVREQDKLWcGIS--DGAIDVVATD 313
Cdd:COG3653 303 AGGldeRLARLRDPATrariraEIEEGLPDNLlgrggwdnilisdSPPNeplvgKSLAEIAAER-GVDpaDAALDLLLEE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 314 HCTFSMAQrlqiskgdFSRCPnglpgvENRMQLLFSSGVMTG-----------------------------RITPERFVE 364
Cdd:COG3653 382 DGRVLIVY--------FIMSE------EDVRELLRHPWVMIGsdgglggkahpraygtfprvlghyvrergVLSLEEAVR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 365 -LTSaMPARLFGLwPQKGLLAPGSDGDVVIIDPrqsqqiqhRHLHDNADY-SPWegftcQGA--IVRTLSRGETIFCDGT 440
Cdd:COG3653 448 kLTS-LPADRLGL-KDRGLLRPGYRADLVVFDP--------ATLADRATFdLPA-----QRAdgIRAVIVNGVVVVEDGK 512
|
570
....*....|....*
gi 90111504 441 FTGkAGRGRFLRRKP 455
Cdd:COG3653 513 PTG-ARPGRVLRGGG 526
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
3-92 |
3.84e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 58.32 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGTVVN--ADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNIDVGIarscddffTGTR 80
Cdd:PRK09237 1 LLLRGGRVIDpaNGIDGVIDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHVYPGSTP--------YGDE 72
|
90
....*....|....*
gi 90111504 81 AAACG---GTTTIID 92
Cdd:PRK09237 73 PDEVGvrsGVTTVVD 87
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
20-92 |
1.78e-08 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 55.80 E-value: 1.78e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111504 20 DLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNIDVgiarscDDFftGTRAAACG---GTTTIID 92
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQGG------TRY--GDRPDMIGvksGVTTVVD 68
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
56-323 |
1.59e-07 |
|
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: 52.72 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 56 VDVHTHF-----------NIDVGIARSC-----DDFFTGTRAAACGGTTTIIDHMGFGPNGCRLRHqLEVYRGYAAHKAV 119
Cdd:cd01292 2 IDTHVHLdgsalrgtrlnLELKEAEELSpedlyEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAA-IEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 120 IDYSFHGVIQHINHA--------ILDEIPMIVEEGLSSFKLYLTYQYKLNDDEVLQ-ALRRLHESGALTTVHPENDAAia 190
Cdd:cd01292 81 IRVVLGLGIPGVPAAvdedaealLLELLRRGLELGAVGLKLAGPYTATGLSDESLRrVLEEARKLGLPVVIHAGELPD-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 191 skraefiaagltapryhalsrplecEAEAIARMINLaqIAGNAPLYIVHlSNGLGLDYLRLARANhqPVWVETCPQYLLL 270
Cdd:cd01292 159 -------------------------PTRALEDLVAL--LRLGGRVVIGH-VSHLDPELLELLKEA--GVSLEVCPLSNYL 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 90111504 271 DERSYdtedgmkfILSPPLRNVREQdklwcgisdGAIDVVATDHCTFSMAQRL 323
Cdd:cd01292 209 LGRDG--------EGAEALRRLLEL---------GIRVTLGTDGPPHPLGTDL 244
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-61 |
2.37e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 52.58 E-value: 2.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111504 3 VLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTH 61
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
5-170 |
2.63e-07 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 52.80 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 5 IKNGTVV----NADGQaKQDLLIESG-IVRQLgnniSPQLPYEEIDATGCYVFPGGVDVHTHF---NIDVGI------AR 70
Cdd:cd01304 1 IKNGTVYdplnGINGE-KMDIFIRDGkIVESS----SGAKPAKVIDASGKVVMAGGVDMHSHIaggKVNVGRilrpedHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 71 SCDDFFTGTRAAACG---GTTTIIdhmgfGPNGCRLrhqlevyrGYAAhkavidySFHGVIQHIN----HAILDEIPMIV 143
Cdd:cd01304 76 RDPVPKGALRRAGVGfsvPSTLAT-----GYRYAEM--------GYTT-------AFEAAMPPLNarhtHEEMADTPILD 135
|
170 180
....*....|....*....|....*..
gi 90111504 144 EEGLSSFKlyltyqyklNDDEVLQALR 170
Cdd:cd01304 136 KGAYPLLG---------NNWFVLEYLR 153
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-98 |
5.17e-07 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 51.75 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 2 RVLIKNGTVVNADGQ----AKQDLLIESGIVRQLGNNISPQLPY---EEIDATGCYVFPGGVDVHTHF--NIDVGIARSC 72
Cdd:COG0402 1 DLLIRGAWVLTMDPAggvlEDGAVLVEDGRIAAVGPGAELPARYpaaEVIDAGGKLVLPGLVNTHTHLpqTLLRGLADDL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 90111504 73 -------------------DDFFTGTRAAAC----GGTTTIIDHMGFGP 98
Cdd:COG0402 81 plldwleeyiwplearldpEDVYAGALLALAemlrSGTTTVADFYYVHP 129
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-190 |
5.69e-07 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 51.33 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPqlPYEEIDATGCYVFPGGVDVHT-------------HFNIDVG 67
Cdd:PRK15446 2 MEMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASA--LPGAIDAEGDYLLPGLVDLHTdnlekhlaprpgvDWPADAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 68 IArSCDdfftgTRAAACGGTT-----TIIDHMGFGPNGCRLRHQL--EVYRGYAAHKAVIDYSFHgvIQH--INHAILDE 138
Cdd:PRK15446 80 LA-AHD-----AQLAAAGITTvfdalSVGDEEDGGLRSRDLARKLidAIEEARARGLLRADHRLH--LRCelTNPDALEL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111504 139 IPMIVEEG-------------------LSSFKLYLTYQYKLNDDEVLQALRRLHESGALTTvhPENDAAIA 190
Cdd:PRK15446 152 FEALLAHPrvdlvslmdhtpgqrqfrdLEKYREYYAGKYGLSDEEFDAFVEERIALSARYA--PPNRRAIA 220
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-61 |
1.75e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 49.71 E-value: 1.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111504 4 LIKNGTVVNADG-QAKQDLLIESGIVRQLGNniSPQLPYEEIDATGCYVFPGGVDVHTH 61
Cdd:COG1820 1 AITNARIFTGDGvLEDGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-92 |
1.90e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 50.00 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVNADGQ----AKQDLLIESGIVRQLGNNISPQlPYEEIDATGCYVFPGGVDVHTH--------------- 61
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAigdlPRGDILIEGDRIAAVAPSIEAP-DAEVVDARGMIVMPGLVDTHRHtwqsvlrgigadwtl 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 90111504 62 ----FNIDVGIA--RSCDDFFTGTRAAAC----GGTTTIID 92
Cdd:PRK08204 81 qtyfREIHGNLGpmFRPEDVYIANLLGALealdAGVTTLLD 121
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-93 |
4.26e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 48.84 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVNADGQ---AKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHfnidvgiarSCDDFFT 77
Cdd:PRK07228 1 MTILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIH---------LCQTLFR 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 90111504 78 G--------------------------TRAAAC--------GGTTTIIDH 93
Cdd:PRK07228 72 GiaddlelldwlkdriwpleaahdaesMYYSALlgigelieSGTTTIVDM 121
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-61 |
5.57e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 48.64 E-value: 5.57e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111504 1 MRVLIKNGTVVNADGQ--AKQDLLIESGIVRQLGNNISPqlPYEE-IDATGCYVFPGGVDVHTH 61
Cdd:PRK08393 1 MSILIKNGYVIYGENLkvIRADVLIEGNKIVEVKRNINK--PADTvIDASGSVVSPGFINAHTH 62
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
4-96 |
7.39e-06 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 47.97 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 4 LIKNGTVVNADGQAKQ---DLLIESGIVRQLGNNISPQLPY--EEIDATGCYVFPGGVDVHTHFNIDV--GIA------- 69
Cdd:cd01298 2 LIRNGTIVTTDPRRVLedgDVLVEDGRIVAVGPALPLPAYPadEVIDAKGKVVMPGLVNTHTHLAMTLlrGLAddlplme 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 90111504 70 ------------RSCDDFFTGTRAAAC----GGTTTIIDHMGF 96
Cdd:cd01298 82 wlkdliwplerlLTEEDVYLGALLALAemirSGTTTFADMYFF 124
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-92 |
6.97e-05 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 44.75 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNGTVVN--ADGQAKQDLLIESGIVRQLGNniSPQLPYEE-IDATGCYVFPGGVDVHTHFnidvgiarscddFFT 77
Cdd:PRK12394 3 NDILITNGHIIDpaRNINEINNLRIINDIIVDADK--YPVASETRiIHADGCIVTPGLIDYHAHV------------FYD 68
|
90 100
....*....|....*....|..
gi 90111504 78 GTR-------AAACGGTTTIID 92
Cdd:PRK12394 69 GTEggvrpdmYMPPNGVTTVVD 90
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
3-61 |
1.68e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 43.97 E-value: 1.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111504 3 VLIKNGTVV--NADGQAKQDLLIESGIVRQLGNNiSPQLPYEEIDATGCYVFPGGVDVHTH 61
Cdd:PRK06038 4 IIIKNAYVLtmDAGDLKKGSVVIEDGTITEVSES-TPGDADTVIDAKGSVVMPGLVNTHTH 63
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
4-93 |
2.11e-04 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 43.39 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 4 LIKNGTVVNADGqAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHfnIDVGiarscddfFTGTRAAA 83
Cdd:cd01293 1 LLRNARLADGGT-ALVDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIH--LDKT--------FTGGRWPN 69
|
90
....*....|
gi 90111504 84 CGGTTTIIDH 93
Cdd:cd01293 70 NSGGTLLEAI 79
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
42-61 |
2.41e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 43.29 E-value: 2.41e-04
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
1-102 |
8.61e-04 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 41.76 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 1 MRVLIKNG-TVVNADGQAKQD----LLIESGIVRQLGNNISPQLPYEE-IDATGCYVFPGGVDVHTHF--NIDVGIARSC 72
Cdd:PRK08203 1 TTLWIKNPlAIVTMDAARREIadggLVVEGGRIVEVGPGGALPQPADEvFDARGHVVTPGLVNTHHHFyqTLTRALPAAQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 90111504 73 D--------------------DFFTGTRAA----ACGGTTTIIDHMGFGPNGCR 102
Cdd:PRK08203 81 DaelfpwlttlypvwarltpeMVRVATQTAlaelLLSGCTTSSDHHYLFPNGLR 134
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
4-61 |
3.84e-03 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 39.66 E-value: 3.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111504 4 LIKNGTVV------NADGQAKQDLLIESGIVRQLGNnISPQLPYEEIDATGCYVFPGGVDVHTH 61
Cdd:PRK12393 5 LIRNAAAImtglpgDAARLGGPDIRIRDGRIAAIGA-LTPLPGERVIDATDCVVYPGWVNTHHH 67
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
4-93 |
3.86e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 39.53 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 4 LIKNGTVVNADGQ----AKQDLLIESGIVRQLGN--NISPQLPYEE-IDATGCYVFPGGVDVHTHFNidVGIARS----- 71
Cdd:PRK07203 3 LIGNGTAITRDPAkpviEDGAIAIEGNVIVEIGTtdELKAKYPDAEfIDAKGKLIMPGLINSHNHIY--SGLARGmmani 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 90111504 72 --CDDFF------------------TGTRAAAC------GGTTTIIDH 93
Cdd:PRK07203 81 ppPPDFIsilknlwwrldraltledVYYSALICsleaikNGVTTVFDH 128
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
357-396 |
4.23e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 39.31 E-value: 4.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 90111504 357 ITPERFVELTSAMPARLFGLWPQKGLLAPGSDGDVVIIDP 396
Cdd:COG1820 322 LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDD 361
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
3-83 |
5.05e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 39.20 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111504 3 VLIKNGT--VVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHfnIDVG--IARS--CDDFF 76
Cdd:PRK07583 23 ALLEGGVppGDTLEGLVLVDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTH--LDKGhiWPRSpnPDGTF 100
|
....*..
gi 90111504 77 TGTRAAA 83
Cdd:PRK07583 101 PGALDAV 107
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
26-65 |
7.00e-03 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 38.45 E-value: 7.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 90111504 26 GIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNID 65
Cdd:cd01309 2 GKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLD 41
|
|
| |
