|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1-428 |
0e+00 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 825.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 1 MSNPIVLKNVRIIDPSRNLDEVGTIIAENGVIFAAGHKAQNQGAPDGAVIRDCTGLVATPGLVDARVHVGEPGGEHRETI 80
Cdd:PRK09059 1 MMRPILLANARIIDPSRGLDEIGTVLIEDGVIVAAGKGAGNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 81 ASASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITKGLAGEEMTEIGLLMQAGAVAFTDAHS 160
Cdd:PRK09059 81 ASASRAAAAGGVTSIIMMPDTDPVIDDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEEMTEFGLLRAAGAVAFTDGRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 161 SVHDTQVLRRIMTYAREFGAVVSCETRDKYLGANGVMHEGLFASWLGLSGIPKEAELIPLERDLRIAQLTRGRYHAAMIS 240
Cdd:PRK09059 161 SVANTQVMRRALTYARDFDAVIVHETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 241 VPESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTK 320
Cdd:PRK09059 241 CAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 321 RLPFSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGLNAGTLKPGAAADIALIDLDEPWLVAKDMLLS 400
Cdd:PRK09059 321 RLPFSEAAAGAIGLETLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGLPAGTLKPGAPADIIVIDLDEPWVVDPEDLKS 400
|
410 420
....*....|....*....|....*...
gi 499970679 401 RSKNTPFEDARFSGRAVATYVSGKLVHA 428
Cdd:PRK09059 401 RSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
6-427 |
2.73e-162 |
|
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: 464.18 E-value: 2.73e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 6 VLKNVRIIDPSRnlDEVGTIIAENGVIFAAGHKAQnqgAPDGAVIRDCTGLVATPGLVDARVHVGEPGGEHRETIASASR 85
Cdd:COG0044 1 LIKNGRVVDPGG--LERADVLIEDGRIAAIGPDLA---APEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 86 AAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITKGLaGEEMTEIGLLMQAGAVAF-----TDAHS 160
Cdd:COG0044 76 AAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAVAFkvfmgSDDGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 161 SVHDTQVLRRIMTYAREFGAVVS--CEtrDKYLGANGVMHEGLFASWLGLSGIPKEAELIPLERDLRIAQLTRGRYHAAM 238
Cdd:COG0044 155 PVLDDGLLRRALEYAAEFGALVAvhAE--DPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 239 ISVPESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVD 318
Cdd:COG0044 233 VSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 319 TKRLPFSEAEDGAIGLETMLAAAL-RLHHGGQVSLMRLIDAMSTRPAQIFGL-NAGTLKPGAAADIALIDLDEPWLVAKD 396
Cdd:COG0044 313 EKELPFAEAPNGIPGLETALPLLLtELVHKGRLSLERLVELLSTNPARIFGLpRKGRIAVGADADLVLFDPDAEWTVTAE 392
|
410 420 430
....*....|....*....|....*....|.
gi 499970679 397 MLLSRSKNTPFEDARFSGRAVATYVSGKLVH 427
Cdd:COG0044 393 DLHSKSKNTPFEGRELTGRVVATIVRGRVVY 423
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
46-419 |
7.55e-155 |
|
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: 442.83 E-value: 7.55e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 46 DGAVIrDCTGLVATPGLVDARVHVGEPGGEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVN 125
Cdd:cd01317 1 DAEVI-DAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 126 VYPAAAITKGLAGEEMTEIGLLMQAGAVAFTDAHSSVHDTQVLRRIMTYAREFGAVVSCETRDKYLGANGVMHEGLFASW 205
Cdd:cd01317 80 VLPIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 206 LGLSGIPKEAELIPLERDLRIAQLTRGRYHAAMISVPESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYP 285
Cdd:cd01317 160 LGLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 286 PLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTKRLPFSEAEDGAIGLETMLAAALR-LHHGGQVSLMRLIDAMSTRPA 364
Cdd:cd01317 240 PLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTlLVKGGLLTLPDLIRALSTNPA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 499970679 365 QIFGLNAGTLKPGAAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVAT 419
Cdd:cd01317 320 KILGLPPGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-427 |
2.28e-141 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 410.36 E-value: 2.28e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 5 IVLKNVRIIDPSrNLDEVGTIIAENGVIFAAGHKAqnqgAPDGAVIRDCTGLVATPGLVDARVHVGEPGGEHRETIASAS 84
Cdd:PRK09357 3 ILIKNGRVIDPK-GLDEVADVLIDDGKIAAIGENI----EAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 85 RAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITKGLAGEEMTEIGLLMQAGAVAFTDAHSSVHD 164
Cdd:PRK09357 78 RAAAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 165 TQVLRRIMTYAREFGAVVS--CEtrDKYLGANGVMHEGLFASWLGLSGIPKEAELIPLERDLRIAQLTRGRYHAAMISVP 242
Cdd:PRK09357 158 ARLMRRALEYAKALDLLIAqhCE--DPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 243 ESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTKRL 322
Cdd:PRK09357 236 GSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKEC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 323 PFSEAEDGAIGLETMLAAAL-RLHHGGQVSLMRLIDAMSTRPAQIFGLNAGTLKPGAAADIALIDLDEPWLVAKDMLLSR 401
Cdd:PRK09357 316 EFEAAPFGITGLETALSLLYtTLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEGEPADLVIFDPEAEWTVDGEDFASK 395
|
410 420
....*....|....*....|....*.
gi 499970679 402 SKNTPFEDARFSGRAVATYVSGKLVH 427
Cdd:PRK09357 396 GKNTPFIGMKLKGKVVYTIVDGKIVY 421
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
5-427 |
3.95e-113 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 338.19 E-value: 3.95e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 5 IVLKNVRIIDPSRNLDEVGTIIAENGVIFAAGHkaqnqgAPDGAVIR---DCTGLVATPGLVDARVHVGEPGGEHRETIA 81
Cdd:PRK07627 3 IHIKGGRLIDPAAGTDRQADLYVAAGKIAAIGQ------APAGFNADktiDASGLIVCPGLVDLSARLREPGYEYKATLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 82 SASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITKGLAGEEMTEIGLLMQAGAVAFTDAHSS 161
Cdd:PRK07627 77 SEMAAAVAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGFSQANVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 162 VHDTQVLRRIMTYAREFGAVVSCETRDKYLGANGVMHEGLFASWLGLSGIPKEAELIPLERDLRIAQLTRGRYHAAMISV 241
Cdd:PRK07627 157 VVDTQVLLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPVAAETIALHTIFELMRVTGARVHLARLSS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 242 PESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTKR 321
Cdd:PRK07627 237 AAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 322 LPFSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGLNAGTLKPGAAADIALIDLDEPWLVAKDMLLSR 401
Cdd:PRK07627 317 LPFAEATPGATGLELLLPLTLKWADEAKVPLARALARITSAPARVLGLPAGRLAEGAPADLCVFDPDAHWRVEPRALKSQ 396
|
410 420
....*....|....*....|....*.
gi 499970679 402 SKNTPFEDARFSGRAVATYVSGKLVH 427
Cdd:PRK07627 397 GKNTPFLGYELPGRVRATLVAGQVAF 422
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
23-426 |
3.07e-104 |
|
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: 315.15 E-value: 3.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 23 GTIIAENGVIFAAGHKAqnqgAPDGAVIRDCTGLVATPGLVDARVHVGEPGGEHRETIASASRAAAAGGVTSIIMMPDTD 102
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLR----IPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 103 PVIDDIALVEFVKKTARDTAAVNVYPAAAITKGLAGEEMTEIGLLMQAGAVA--FTDAHSSVHDTQVLRRIMTYAREFGA 180
Cdd:TIGR00857 82 PPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGrmFTDDGSEVQDILSMRRALEYAAIAGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 181 VVSCETRDKYLGANGVMHEGLFASWLGLSGIPKEAELIPLERDLRIAQLTRGRYHAAMISVPESVEAIERARSRGAKVTC 260
Cdd:TIGR00857 162 PIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 261 GISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTKRLPFSEAEDGAIGLETMLAA 340
Cdd:TIGR00857 242 EVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 341 ALRLHHGGQVSLMRLIDAMSTRPAQIFGL-NAGTLKPGAAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVAT 419
Cdd:TIGR00857 322 LLQLLVKGLISLKDLIRMLSINPARIFGLpDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIAT 401
|
....*..
gi 499970679 420 YVSGKLV 426
Cdd:TIGR00857 402 ILRGKVV 408
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
1-421 |
5.43e-97 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 296.90 E-value: 5.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 1 MSNpIVLKNVRIIDPSRNLDEVGTIIAENGVIFAAGhkAQNQGAPDGAVIRDCTGLVATPGLVDARVHVGEPGGEHRETI 80
Cdd:PRK07369 1 MSN-ELLQQVRVLDPVSNTDRIADVLIEDGKIQAIE--PHIDPIPPDTQIIDASGLILGPGLVDLYSHSGEPGFEERETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 81 ASASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITKGLAGEEMTEIGLLMQAGAVAFTDAHs 160
Cdd:PRK07369 78 ASLAAAAAAGGFTRVAILPDTFPPLDNPATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTELAELAAAGVVGFTDGQ- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 161 SVHDTQVLRRIMTYAREFG---AVVSCetrDKYLGANGVMHEGLFASWLGLSGIPKEAELIPLERDLRIAQLTRGRYHAA 237
Cdd:PRK07369 157 PLENLALLRRLLEYLKPLGkpvALWPC---DRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 238 MISVPESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDV 317
Cdd:PRK07369 234 RISTARSVELIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 318 DTKRLPFSEAEDGAIGLEtmLAAAL---RLHHGGQVSLMRLIDAMSTRPAQIFGLNAGTLKPGAAADIALIDLDEPWLVA 394
Cdd:PRK07369 314 EEKTVAFAEAPPGAIGLE--LALPLlwqNLVETGELSALQLWQALSTNPARCLGQEPPSLAPGQPAELILFDPQKTWTVS 391
|
410 420
....*....|....*....|....*..
gi 499970679 395 KDMLLSRSKNTPFEDARFSGRAVATYV 421
Cdd:PRK07369 392 AQTLHSLSRNTPWLGQTLKGRVLQTWV 418
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
55-423 |
2.06e-61 |
|
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: 202.95 E-value: 2.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 55 GLVATPGLVDARVHVGEPGGEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITK 134
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 135 GLAGEEMTEIGLlmqAGAVAFTDahSSV----HDTQVLRRI--MTYARefgAVVSCETRDkylgangvMHEGLFASWLGL 208
Cdd:cd01318 81 SEDLEELDKAPP---AGYKIFMG--DSTgdllDDEETLERIfaEGSVL---VTFHAEDED--------RLRENRKELKGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 209 SGIPK----EAELIPLERDLRIAQLTRGRYHAAMISVPESVEAIERARSRgakVTCGISINNLALNENDIGEYRTFFKLY 284
Cdd:cd01318 145 SAHPRirdaEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLGTLGKVN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 285 PPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTKRLPFSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPA 364
Cdd:cd01318 222 PPLRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPA 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 365 QIFGL-NAGTLKPGAAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSG 423
Cdd:cd01318 302 RIFGIkNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
56-419 |
3.95e-57 |
|
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: 191.07 E-value: 3.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 56 LVATPGLVDARVHVGEPG-GEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITK 134
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGgTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 135 GLAGEEMTEiglLMQAGAVAF------TDAHSSVHDTQVLRRIMTYAREFGAVVscetrdkylgangVMHeglfaswlgl 208
Cdd:cd01302 81 GDVTDELKK---LFDAGINSLkvfmnyYFGELFDVDDGTLMRTFLEIASRGGPV-------------MVH---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 209 sgipkeaelipLERDLRIAQLTRGRYHAAMISVPESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLR 288
Cdd:cd01302 135 -----------AERAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPPLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 289 PEDDRVAMADAVASGAIDIIVSSHDPQDVDTKRLP--FSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQI 366
Cdd:cd01302 204 SKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGkdIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARI 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 499970679 367 FGL-NAGTLKPGAAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVAT 419
Cdd:cd01302 284 FGLyPKGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
6-428 |
1.33e-55 |
|
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: 190.19 E-value: 1.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 6 VLKNVRIIDPsrNLDEVGTIIAENGVIFAAGHKAQNqgaPDGAVIRDCTGLVATPGLVDARVHVGEPGGEHRETIASASR 85
Cdd:cd01315 3 VIKNGRVVTP--DGVREADIAVKGGKIAAIGPDIAN---TEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 86 AAAAGGVTSIIMMP-DTDPVIDDIALVEFVKKTARDTAAVNVypaaAITKGLAGEEMTEIGLLMQAGAVAF--------T 156
Cdd:cd01315 78 AAAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDV----GFWGGLVPGNLDQLRPLDEAGVVGFkcflcpsgV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 157 DAHSSVHDTQVLrRIMTYAREFGAV--VSCE--TRDKYLGANGVMHEGlfASWLG-LSGIPKEAELIPLERDLRIAQLTR 231
Cdd:cd01315 154 DEFPAVDDEQLE-EAMKELAKTGSVlaVHAEnpEITEALQEQAKAKGK--RDYRDyLASRPVFTEVEAIQRILLLAKETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 232 GRYHAAMISVPESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSS 311
Cdd:cd01315 231 CRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 312 HDPQDVDTKRLP---FSEAEDGAIGLET----MLAAAlrLHHGGqVSLMRLIDAMSTRPAQIFGLNA--GTLKPGAAADI 382
Cdd:cd01315 311 HSPCTPELKLLGkgdFFKAWGGISGLQLglpvMLTEA--VNKRG-LSLEDIARLMCENPAKLFGLSHqkGRIAVGYDADF 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 499970679 383 ALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSGKLVHA 428
Cdd:cd01315 388 VVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQ 433
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-426 |
1.14e-51 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 179.85 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 1 MSNpIVLKNVRIidPSRNLDEVGTIIAENGVIFAAGhkAQNQGAPDGAVIrDCTGLVATPGLVDARVHVGEPGGEHRETI 80
Cdd:PRK02382 1 MRD-ALLKDGRV--YYNNSLQPRDVRIDGGKITAVG--KDLDGSSSEEVI-DARGMLLLPGGIDVHVHFREPGYTHKETW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 81 ASASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVypaaAITKGLaGEEMTEIGLLMQAGAVAFTD--- 157
Cdd:PRK02382 75 YTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDF----GINGGV-TGNWDPLESLWERGVFALGEifm 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 158 AHSSVH---DTQVLRRIMTYAREFGAVVSCETRDKYL---GANGVMHEGLFASWlglSGI-PKEAELIPLERDLRIAQLT 230
Cdd:PRK02382 150 ADSTGGmgiDEELFEEALAEAARLGVLATVHAEDEDLfdeLAKLLKGDADADAW---SAYrPAAAEAAAVERALEVASET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 231 RGRYHAAMISVPESVEAIerarsRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVS 310
Cdd:PRK02382 227 GARIHIAHISTPEGVDAA-----RREGITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVAS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 311 SHDPQDVDTKRLPFSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGLNA-GTLKPGAAADIALIDLDE 389
Cdd:PRK02382 302 DHAPHTREEKDADIWDAPSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLDGkGRIAEGYDADLVLVDPDA 381
|
410 420 430
....*....|....*....|....*....|....*....
gi 499970679 390 PWLVAKDMLLSRSKNTPFE--DARFSgraVATYVSGKLV 426
Cdd:PRK02382 382 AREIRGDDLHSKAGWTPFEgmEGVFP---ELTMVRGTVV 417
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
46-389 |
1.50e-50 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 175.28 E-value: 1.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 46 DGAVIRDCTGLVATPGLVDARVHVgePGGE-HRETIASASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKkTARDTAAV 124
Cdd:PRK08417 16 KGEEILDAKGKTLLPALVDLNVSL--KNDSlSSKNLKSLENECLKGGVGSIVLYPDSTPAIDNEIALELIN-SAQRELPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 125 NVYPAAAITKglAGEEMTEIGLLMQAGAVAFtdAHSSVHDTQVLRRIMTYAREFGAVVSCETRDKYLGANGVMHEGLFAS 204
Cdd:PRK08417 93 QIFPSIRALD--EDGKLSNIATLLKKGAKAL--ELSSDLDANLLKVIAQYAKMLDVPIFCRCEDSSFDDSGVMNDGELSF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 205 WLGLSGIPKEAELIPLERDLRIAQLTRGRYHAAMISVPESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLY 284
Cdd:PRK08417 169 ELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNTAAKLN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 285 PPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTKRLPFSEAEDGAIGLETMLAAAL-RLHHGGQVSLMRLIDAMSTRP 363
Cdd:PRK08417 249 PPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYtYLVKEGIITWSELSRFTSYNP 328
|
330 340
....*....|....*....|....*.
gi 499970679 364 AQIFGLNAGTLKPGAAADIALIDLDE 389
Cdd:PRK08417 329 AQFLGLNSGEIEVGKEADLVLFDPNE 354
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
44-428 |
1.58e-44 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 160.64 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 44 APDGAVIrDCTGLVATPGLVDARVHVGEPGGEHRETIASASRAAAAGGVTSIIMMP--DTDPVIDDIALvEFVKKTARDT 121
Cdd:PRK06189 39 SPAREII-DADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlnSIPPTVTREAL-DAKAELARQK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 122 AAVNVypaaAITKGLAGEEMTEIGLLMQAGAVAF--------TDAHSSVHDTQVLRRiMTYAREFGAVVSCETRDKYLGA 193
Cdd:PRK06189 117 SAVDF----ALWGGLVPGNLEHLRELAEAGVIGFkafmsnsgTDEFRSSDDLTLYEG-MKEIAALGKILALHAESDALTR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 194 NGVM---HEGLFASWLGLSGIPKEAELIPLERDLRIAQLTRGRYHAAMISVPESVEAIERARSRGAKVTCGISINNLALN 270
Cdd:PRK06189 192 HLTTqarQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 271 ENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTKR-LPFSEAEDGAIGLETMLAAALRL-HHGG 348
Cdd:PRK06189 272 EEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPCPPELKEgDDFFLVWGGISGGQSTLLVMLTEgYIER 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 349 QVSLMRLIDAMSTRPAQIFGL-NAGTLKPGAAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSGKLVH 427
Cdd:PRK06189 352 GIPLETIARLLATNPAKRFGLpQKGRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVY 431
|
.
gi 499970679 428 A 428
Cdd:PRK06189 432 Q 432
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-426 |
2.34e-40 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 149.05 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 1 MSNPIVLKNVRIIDPSRNLDeVGTIIAENGVIFAAghkAQNQGAPDGAVIRDCTGLVATPGLVDARVHVGEPGGEHRETI 80
Cdd:PRK07575 1 MMMSLLIRNARILLPSGELL-LGDVLVEDGKIVAI---APEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 81 ASASRAAAAGGVTSIIMMPDTDPVIDDIALVEfvKKTARdtaavnvypaaAITKGLA------GEEMTEIGLLMQA---- 150
Cdd:PRK07575 77 FTASRACAKGGVTSFLEMPNTKPLTTTQAALD--DKLAR-----------AAEKCVVnygffiGATPDNLPELLTAnptc 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 151 GAVAFTDAHSS---VHDTQVLRRIMTYAREFGAVvSCE-------TRDKYLGANGV-MHeglfaswlglSGI-PKEAELI 218
Cdd:PRK07575 144 GIKIFMGSSHGpllVDEEAALERIFAEGTRLIAV-HAEdqariraRRAEFAGISDPaDH----------SQIqDEEAALL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 219 PLERDLRIAQLTRGRYHAAMISVPESVEAIerARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMAD 298
Cdd:PRK07575 213 ATRLALKLSKKYQRRLHILHLSTAIEAELL--RQDKPSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 299 AVASGAIDIIVSSHDPQDVDTKRLPFSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGL-NAGTLKPG 377
Cdd:PRK07575 291 ALRDGVIDFIATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGIpNKGRIAPG 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 499970679 378 AAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSGKLV 426
Cdd:PRK07575 371 YDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIV 419
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
6-426 |
1.00e-37 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 141.06 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 6 VLKNVRIIDpsrnldevGTIIAENGVIFAAGHKAQNqgapdGAVIRDCTGLVATPGLVDARVHVGEPGGEHRETIASASR 85
Cdd:PRK04250 6 FLLKGRIVE--------GGIGIENGRISKISLRDLK-----GKEVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 86 AAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNvYPAAAITKGLAGE------EMTEIGLLMQAGAVAFTDAH 159
Cdd:PRK04250 73 AALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYAD-YALNFLIAGNCEKaeeikaDFYKIFMGASTGGIFSENFE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 160 SSvhdtqvlrrimtYAREFGaVVSCETRDKYLGANGVMHeglfaswlglsgiPKEAELIPLERDLRIAQLTRGRYHAAMI 239
Cdd:PRK04250 152 VD------------YACAPG-IVSVHAEDPELIREFPER-------------PPEAEVVAIERALEAGKKLKKPLHICHI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 240 SVPESVEAIerARSRGAKVTCGISINNLALNENDIgEYRTFFKLYPPLRPEDDRVAMADAVASgaIDIIVSSHDPQDVDT 319
Cdd:PRK04250 206 STKDGLKLI--LKSNLPWVSFEVTPHHLFLTRKDY-ERNPLLKVYPPLRSEEDRKALWENFSK--IPIIASDHAPHTLED 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 320 KRlpfsEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGLNAGTLKPGAAADIALIDLDEPWLVAKDMLL 399
Cdd:PRK04250 281 KE----AGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNYGIEEGNYANFAVFDMKKEWTIKAEELY 356
|
410 420
....*....|....*....|....*..
gi 499970679 400 SRSKNTPFEDARFSGRAVATYVSGKLV 426
Cdd:PRK04250 357 TKAGWTPYEGFKLKGKVIMTILRGEVV 383
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
3-426 |
6.48e-37 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 140.01 E-value: 6.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 3 NPIVLKNVRIIDPSRNLDevGTIIAENGVIfaAGHKAQNQGAPDGAVIrDCTGLVATPGLVDARVHVGEPGGEHRETIAS 82
Cdd:PRK09236 2 KRILIKNARIVNEGKIFE--GDVLIENGRI--AKIASSISAKSADTVI-DAAGRYLLPGMIDDQVHFREPGLTHKGDIAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 83 ASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNvYpaaAITKGLAGEEMTEIGLL---MQAGAVAFTDAH 159
Cdd:PRK09236 77 ESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLAN-Y---SFYFGATNDNLDEIKRLdpkRVCGVKVFMGAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 160 SS---VHDTQVLRRIMTYArEFGAVVSCE-------TRDKYLGANGvmheglfaswlglSGIPkeAELIPLERD------ 223
Cdd:PRK09236 153 TGnmlVDNPETLERIFRDA-PTLIATHCEdtptikaNLAKYKEKYG-------------DDIP--AEMHPLIRSaeacyk 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 224 -----LRIAQLTRGRYHAAMISVPESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMAD 298
Cdd:PRK09236 217 ssslaVSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 299 AVASGAIDIIVSSHDPQDVDTKRLPFSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGL-NAGTLKPG 377
Cdd:PRK09236 297 ALADDRIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDIkERGFIREG 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 499970679 378 AAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSGKLV 426
Cdd:PRK09236 377 YWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLV 425
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
23-429 |
5.76e-36 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 137.29 E-value: 5.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 23 GTIIAENG------VIFAAGHKAQNQGAPDGAVIRDCTGLVATPGLVDARVHVGEPGGEHRETIASASRAAAAGGVTSII 96
Cdd:PRK08044 10 GTVILENEarvvdiAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 97 MMP-DTDPVIDDIALVEFVKKTARDTAAVNvypaAAITKGLAGEEMTEIGLLMQAGAVAFT------------DAHSSVH 163
Cdd:PRK08044 90 EMPlNQLPATVDRASIELKFDAAKGKLTID----AAQLGGLVSYNLDRLHELDEVGVVGFKcfvatcgdrgidNDFRDVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 164 DTQVLRRIMTYArEFGAVVS--CETR---DKyLGANGvMHEGLFASWLGLSGIPKEAELIPLERDLRIAQLTRGRYHAAM 238
Cdd:PRK08044 166 DWQFYKGAQKLG-ELGQPVLvhCENAlicDE-LGEEA-KREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 239 ISVPESVEAIERARSRGAKVTCGISINNLALNENDIGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVD 318
Cdd:PRK08044 243 ISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 319 TKRLPFSEAEDGAIGLET----MLAAALRLHHggqVSLMRLIDAMSTRPAQIFGL-NAGTLKPGAAADIALIDLDEPWLV 393
Cdd:PRK08044 323 MKAGNIMEAWGGIAGLQNcmdvMFDEAVQKRG---MSLPMFGKLMATNAADIFGLqQKGRIAPGKDADFVFIQPNSSYVL 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 499970679 394 AKDMLLSRSKNTPFEDARFSGRAVATYVSGKLVHAI 429
Cdd:PRK08044 400 KNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDI 435
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
6-426 |
2.36e-35 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 135.43 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 6 VLKNVRIIDPsrNLDEVGTIIAENGVIFAAGHKAQnqgAPDGAVIrDCTGLVATPGLVDARVHVGEPGGEHRETIASASR 85
Cdd:PRK09060 8 ILKGGTVVNP--DGEGRADIGIRDGRIAAIGDLSG---ASAGEVI-DCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 86 AAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVypaaAITKGLAGEEMTEIGLLMQAGAVA----FtdAHSS 161
Cdd:PRK09060 82 AAVLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDF----AFYVGGTRDNADELAELERLPGCAgikvF--MGSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 162 -----VHDTQVLRRIMTYAREFGAVVScetRDKY-LGAN-GVMHEGLFAS---WLGlsgipKEAELIPLERDLRIAQLTR 231
Cdd:PRK09060 156 tgdllVEDDEGLRRILRNGRRRAAFHS---EDEYrLRERkGLRVEGDPSShpvWRD-----EEAALLATRRLVRLARETG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 232 GRYHAAMISVPESVEAIERARSRgakVTCGISINNLALNENDIGE-YRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVS 310
Cdd:PRK09060 228 RRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLAAPECYErLGTLAQMNPPIRDARHRDGLWRGVRQGVVDVLGS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 311 SHDPQDVDTKRLPFSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGL-NAGTLKPGAAADIALIDLDE 389
Cdd:PRK09060 305 DHAPHTLEEKAKPYPASPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIaGKGRIAVGYDADFTIVDLKR 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 499970679 390 PWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSGKLV 426
Cdd:PRK09060 385 RETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRV 421
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
5-426 |
1.83e-31 |
|
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: 124.64 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 5 IVLKNVRIIDPSR--NLDevgtIIAENGVIFAAGhkaQNQGAPDGAVIRDCTGLVATPGLVDARVHVGEP--GGEHRETI 80
Cdd:cd01314 1 LIIKNGTIVTADGsfKAD----ILIEDGKIVAIG---PNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 81 ASASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITKglAGEEMT-EIGLLMQAGAVAF---- 155
Cdd:cd01314 74 ESGTRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITD--WTDSVIeELPELVKKGISSFkvfm 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 156 TDAHSSVHDTQVLRRIMTYAREFGAV--VSCEtrdkylgaNGVMHEGLFASWL--GLSGiPK----------EAELIplE 221
Cdd:cd01314 152 AYKGLLMVDDEELLDVLKRAKELGALvmVHAE--------NGDVIAELQKKLLaqGKTG-PEyhalsrppevEAEAT--A 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 222 RDLRIAQLTRGRYHAAMISVPESVEAIERARSRGAKV---TCgisINNLALNENDIGEYRTFFKLY---PPLRPEDDRVA 295
Cdd:cd01314 221 RAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVygeTC---PQYLLLDDSDYWKDWFEGAKYvcsPPLRPKEDQEA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 296 MADAVASGAIDIIVSSHDPQDVDTKRL---PFSEAEDGAIGLETMLAaaLRLHHG---GQVSLMRLIDAMSTRPAQIFGL 369
Cdd:cd01314 298 LWDGLSSGTLQTVGSDHCPFNFAQKARgkdDFTKIPNGVPGVETRMP--LLWSEGvakGRITLEKFVELTSTNPAKIFGL 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 499970679 370 --NAGTLKPGAAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSGKLV 426
Cdd:cd01314 376 ypRKGTIAVGSDADLVIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVV 434
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
56-426 |
3.40e-31 |
|
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: 122.17 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 56 LVATPGLVDARVHVGEPGGEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAV--NVYPAAAIT 133
Cdd:cd01316 2 TIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCdyAFSIGATST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 134 KG-----LAGEEMteiGLLMqagavaftdAHSSVHDTQVLRRIMTYAREFGAvvscetrdkylgangvmheglfasWLGL 208
Cdd:cd01316 82 NAatvgeLASEAV---GLKF---------YLNETFSTLILDKITAWASHFNA------------------------WPST 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 209 SGIPKEAELIPLERDLRIAQLTRGRYHAAMISVPESVEAIERARSRGAKVTCGISINNLALNENDIGeyRTFFKLYPPLR 288
Cdd:cd01316 126 KPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLP--RGQYEVRPFLP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 289 PEDDRVAMADAVASgaIDIIVSSHDPQDVDTKRlpFSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFG 368
Cdd:cd01316 204 TREDQEALWENLDY--IDCFATDHAPHTLAEKT--GNKPPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFN 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 499970679 369 LnagtlkPGAAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSGKLV 426
Cdd:cd01316 280 L------PPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETA 331
|
|
| PLN02795 |
PLN02795 |
allantoinase |
57-428 |
7.33e-29 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 118.34 E-value: 7.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 57 VATPGLVDARVHVGEPGGEHRETIASASRAAAAGGVTSIIMMP-DTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITKG 135
Cdd:PLN02795 96 VVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 136 LAGEEmTEIGLLMQAGAVAFT-----------DAHSSVHDTQVLRRIMTYAREF---GAVVSCETRDKYLGANGVMHEGL 201
Cdd:PLN02795 176 NAHNA-SVLEELLDAGALGLKsfmcpsgindfPMTTATHIKAALPVLAKYGRPLlvhAEVVSPVESDSRLDADPRSYSTY 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 202 FAS----WlglsgiPKEA--ELIPLERDLRIAQLTRG-RYHAAMIS-VPESVEAIERARSRGAKVTCGISINNLALNEND 273
Cdd:PLN02795 255 LKSrppsW------EQEAirQLLEVAKDTRPGGVAEGaHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSAEE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 274 IGEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTKRLP---FSEAEDGAIGLETMLAAALRLHHGGQV 350
Cdd:PLN02795 329 IPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEegnFLRAWGGISSLQFVLPATWTAGRAYGL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 351 SLMRLIDAMSTRPAQIFGLNA-GTLKPGAAADI------ALIDLDEPWLVakdmLLSRSKNTPFEDARFSGRAVATYVSG 423
Cdd:PLN02795 409 TLEQLARWWSERPAKLAGLDSkGAIAPGKDADIvvwdpeAEFVLDESYPI----YHKHKSLSPYLGTKLSGKVIATFVRG 484
|
....*
gi 499970679 424 KLVHA 428
Cdd:PLN02795 485 NLVFL 489
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
5-428 |
2.53e-21 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 95.62 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 5 IVLKNVRIIDPSRnlDEVGTIIAENGVIFAAGhkaqnqgAPDGAVIRDCTGLVATPGLVDARVHVGEP-GGEH-RETIAS 82
Cdd:PRK08323 3 TLIKNGTVVTADD--TYKADVLIEDGKIAAIG-------ANLGDEVIDATGKYVMPGGIDPHTHMEMPfGGTVsSDDFET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 83 ASRAAAAGGVTSIIMMPDTDPVIDDIALVEFVKKTARDTAAVNVYPAAAITkGLAGEEMTEIGLLMQAGAVAFT-----D 157
Cdd:PRK08323 74 GTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIIT-DWNEVVLDEMPELVEEGITSFKlfmayK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 158 AHSSVHDTQVLRrIMTYAREFGAV--VSCETRD------KYLGANG----VMHeglfaswlGLSGIPK-EAELIplERDL 224
Cdd:PRK08323 153 GALMLDDDELLR-ALQRAAELGALpmVHAENGDaiaylqAKLLAEGktgpEYH--------ALSRPPEvEGEAT--NRAI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 225 RIAQLTRGRYHAAMISVPESVEAIERARSRGAKV---TCgisINNLALNENDIGEYRTF----FKLYPPLRPEDDRVAMA 297
Cdd:PRK08323 222 MLAELAGAPLYIVHVSCKEALEAIRRARARGQRVfgeTC---PQYLLLDESEYDGPDWFegakYVMSPPLRDKEHQDALW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 298 DAVASGAIDIIVSSHDP----QDVDTKRLPFSEAEDGAIGLETMLAaaLRLHHG---GQVSLMRLIDAMSTRPAQIFGL- 369
Cdd:PRK08323 299 RGLQDGDLQVVATDHCPfcfeQKKQLGRGDFTKIPNGTPGVEDRMP--LLFSEGvmtGRITLNRFVELTSTNPAKIFGLy 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 370 -NAGTLKPGAAADIALIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSGKLVHA 428
Cdd:PRK08323 377 pRKGTIAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVE 436
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
21-412 |
7.84e-21 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 93.77 E-value: 7.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 21 EVGTIIAENGVIFAAGHKAQNQGAP--DGAVIrdctglvatPGLVDARVHVGEPGGEHRETIASASRAAAAGGVTSIIMM 98
Cdd:PRK01211 14 DYLEIEVEDGKIKSIKKDAGNIGKKelKGAIL---------PAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 99 PDTDPVIDDIAlvEFVKKTARdtaavnVYPAAAITKGLAGEEMTEIGLLMQAGAVAF-------TDAHSSVHDTQVLRRI 171
Cdd:PRK01211 85 PNNNIPIKDYN--AFSDKLGR------VAPKAYVDFSLYSMETGNNALILDERSIGLkvymggtTNTNGTDIEGGEIKKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 172 --MTYAREFGAVVSCETRDKYLGANGVMHEGLfaswlglsGIPKEAELIPLERdlrIAQLTRGRYHAAMISVPESVEAIE 249
Cdd:PRK01211 157 neANIPVFFHAELSECLRKHQFESKNLRDHDL--------ARPIECEIKAVKY---VKNLDLKTKIIAHVSSIDVIGRFL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 250 RArsrgakvtcgISINNLALN-ENDIGeyrTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQDVDTKRlPFSEAE 328
Cdd:PRK01211 226 RE----------VTPHHLLLNdDMPLG---SYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ-EFEYAK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 329 DGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGLNAGTLKPGAAADIALIDLDEPWLVAKDMLLSRSKNTPFE 408
Cdd:PRK01211 292 SGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFN 371
|
....*.
gi 499970679 409 --DARF 412
Cdd:PRK01211 372 gfDAIF 377
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
42-426 |
3.16e-20 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 92.45 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 42 QGAPDGAVIRDCTGLVATPGLVDARVHVGEPGGE---HRETIASASRAAAAGGVTSII--MMPDTDPVIDDIalVEFVKK 116
Cdd:PRK13404 36 EGLGPGAREIDATGRLVLPGGVDSHCHIDQPSGDgimMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSLREA--VEDYHR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 117 TARDTAAVNV---YPAAAITKGLAGEEMTEiglLMQAGAVAF----TDAHSSVHDTQVLRrIMTYAREFGAV--VSCETR 187
Cdd:PRK13404 114 RAAGKAVIDYafhLIVADPTEEVLTEELPA---LIAQGYTSFkvfmTYDDLKLDDRQILD-VLAVARRHGAMvmVHAENH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 188 D--KYLgANGVMHEGLFASWLGLSGIPKEAELIPLERDLRIAQLTRGRYHAAMISVPESVEAIERARSRGAKV---TCGi 262
Cdd:PRK13404 190 DmiAWL-TKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIfaeTCP- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 263 siNNLALNENDI---GEYRTFFKLYPPLRPEDDRVAMADAVASGAIDIIVSSHDP---QDVDTKRL-----PFSEAEDGA 331
Cdd:PRK13404 268 --QYLFLTAEDLdrpGMEGAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAPfrfDDTDGKLAaganpSFKAIANGI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 332 IGLETMLAaaLRLHHG---GQVSLMRLIDAMSTRPAQIFGLNA--GTLKPGAAADIALIDLDEPWLVAKDMLLSRSKNTP 406
Cdd:PRK13404 346 PGIETRLP--LLFSEGvvkGRISLNRFVALTSTNPAKLYGLYPrkGAIAIGADADIAIWDPDREVTITNADLHHAADYTP 423
|
410 420
....*....|....*....|
gi 499970679 407 FEDARFSGRAVATYVSGKLV 426
Cdd:PRK13404 424 YEGMRVTGWPVTVLSRGRVV 443
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
55-426 |
8.23e-17 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 81.73 E-value: 8.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 55 GLVATPGLVDARVHVGEPGGEHRETIASASRAAAAGGVTSIIMMPDTDPVID-----DIALVEFVKKTARDTAavnVYpa 129
Cdd:PRK00369 42 GTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNtpeaiTEKLAELEYYSRVDYF---VY-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 130 AAITKGLagEEMTEIGLlmqAGAVAFTDahsSVHDTQVLRRIMTYAREfgAVVSCETRDKYLGANGVMHeglfaswlgls 209
Cdd:PRK00369 117 SGVTKDP--EKVDKLPI---AGYKIFPE---DLEREETFRVLLKSRKL--KILHPEVPLALKSNRKLRR----------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 210 GIPKEAELIPLERDLRiaqltrgRYHAAMISVPESVEAierARSRGAkvTCGISINNLALNendiGEYRTFFKLYPPLRP 289
Cdd:PRK00369 176 NCWYEIAALYYVKDYQ-------NVHITHASNPRTVRL---AKELGF--TVDITPHHLLVN----GEKDCLTKVNPPIRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 290 EDDRVAMADAVASgaIDIIVSSHDPQDVDTKRLPFSEAEDGAIGLETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGL 369
Cdd:PRK00369 240 INERLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGI 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 499970679 370 NAGTLKPGAAADIALIDLdEPWLVAKDmlLSRSKNTPFEDARFSGRAVATYVSGKLV 426
Cdd:PRK00369 318 PYGEIKEGYRANFTVIQF-EDWRYSTK--YSKVIETPLDGFELKASVYATIVQGKLA 371
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
21-426 |
8.52e-10 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 60.63 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 21 EVGTIIAENGVIFAAGhkaQNQGAPDGAVIRDCTGLVATPGLVDARVHVGEP--GGEHRETIASASRAAAAGGVTSIImm 98
Cdd:PLN02942 21 ELADVYVEDGIIVAVA---PNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTMHI-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 99 pdtDPVI----DDIALVEFVKKTARDtAAVNVYPAAAITKgLAGEEMTEIGLLMQAGAV---AFTDAHSS---VHDTQVL 168
Cdd:PLN02942 96 ---DFVIpvngNLLAGYEAYEKKAEK-SCMDYGFHMAITK-WDDTVSRDMETLVKEKGInsfKFFMAYKGslmVTDELLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 169 RRIMTyAREFGAV--VSCETRDKYLGANGVMHEglfaswLGLSGI-------PKEAELIPLERDLRIAQLTRGRYHAAMI 239
Cdd:PLN02942 171 EGFKR-CKSLGALamVHAENGDAVFEGQKRMIE------LGITGPeghalsrPPLLEGEATARAIRLAKFVNTPLYVVHV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 240 SVPESVEAIERARSRGAKVTCGISINNLALNENDI--GEYRTFFK--LYPPLRPEDDRVAMADAVASGAIDIIVSSHDPQ 315
Cdd:PLN02942 244 MSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLwdPDFTIASKyvMSPPIRPAGHGKALQAALSSGILQLVGTDHCPF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 316 DVDTKRL---PFSEAEDGAIGLETmlaaalRLH-------HGGQVSLMRLIDAMSTRPAQIFGL--NAGTLKPGAAADIA 383
Cdd:PLN02942 324 NSTQKAFgkdDFRKIPNGVNGIEE------RMHlvwdtmvESGQISPTDYVRVTSTECAKIFNIypRKGAILAGSDADII 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 499970679 384 LIDLDEPWLVAKDMLLSRSKNTPFEDARFSGRAVATYVSGKLV 426
Cdd:PLN02942 398 ILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVV 440
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-78 |
1.40e-09 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 59.59 E-value: 1.40e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499970679 1 MSNPIVLKNVRIID-PSRNLDEVGTIIAENGVIFAAGHKAQNQgAPDGAVIRDCTGLVATPGLVDARVHVGEPGGEHRE 78
Cdd:COG1228 6 QAGTLLITNATLVDgTGGGVIENGTVLVEDGKIAAVGPAADLA-VPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVE 83
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-69 |
1.63e-09 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 59.03 E-value: 1.63e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499970679 4 PIVLKNVRIIDPSRNLDEVGTIIAENGVIFAAGHkaqNQGAPDGAVIRDCTGLVATPGLVDARVHV 69
Cdd:COG3964 1 DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAK---DIDAAEAKKVIDASGLYVTPGLIDLHTHV 63
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
5-426 |
6.64e-09 |
|
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: 57.31 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 5 IVLKNVRIIDPSRNLDEVGTIIAENGVIFAAGhkaqNQGAPDGAVIRDCTGLVATPGLVDARVHvgepgGEHRETIASAS 84
Cdd:cd01297 2 LVIRNGTVVDGTGAPPFTADVGIRDGRIAAIG----PILSTSAREVIDAAGLVVAPGFIDVHTH-----YDGQVFWDPDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 85 RAAAAGGVTSIIMM---------------PDTDPVIDDIALV-----------EFVKKTARDTAAVNV---YPAAAITK- 134
Cdd:cd01297 73 RPSSRQGVTTVVLGncgvspapanpddlaRLIMLMEGLVALGeglpwgwatfaEYLDALEARPPAVNVaalVGHAALRRa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 135 --GLAGEEMT--EIGLL-------MQAGAVAF----TDAHSSVHDTQVLRRIMTYAREFGAVVscetrdkylgangVMHE 199
Cdd:cd01297 153 vmGLDAREATeeELAKMrellreaLEAGALGIstglAYAPRLYAGTAELVALARVAARYGGVY-------------QTHV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 200 GLFAswlglsgipkEAELIPLERDLRIAQLTRGRYHAAMISV---------PESVEAIERARSRGAKVTCGIsinnlaln 270
Cdd:cd01297 220 RYEG----------DSILEALDELLRLGRETGRPVHISHLKSagapnwgkiDRLLALIEAARAEGLQVTADV-------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 271 endigeyrtffklYP-PLRPEDDRVAMAdavasgaidiivsSHDPQDVDTKRLPFSEAEDGAIGletmlAAALRLHH--- 346
Cdd:cd01297 282 -------------YPyGAGSEDDVRRIM-------------AHPVVMGGSDGGALGKPHPRSYG-----DFTRVLGHyvr 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 347 -GGQVSLMRLIDAMSTRPAQIFGL-NAGTLKPGAAADIALIDLDEPWLVAkdmllsrskntPFED-ARFSGRAVATYVSG 423
Cdd:cd01297 331 eRKLLSLEEAVRKMTGLPARVFGLaDRGRIAPGYRADIVVFDPDTLADRA-----------TFTRpNQPAEGIEAVLVNG 399
|
...
gi 499970679 424 KLV 426
Cdd:cd01297 400 VPV 402
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-69 |
4.36e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.77 E-value: 4.36e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499970679 5 IVLKNVRIIDPSRNLDEVGTIIAENGVIFAAGhkaQNQGAPDGAVIRDCTGLVATPGLVDARVHV 69
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGVIDIAIEDGKIAAVA---GDIDGSQAKKVIDLSGLYVSPGWIDLHVHV 62
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
57-426 |
4.68e-07 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 51.35 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 57 VATPGLVDARVH--------VGEPGGEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDIALVEF----------VKKTA 118
Cdd:pfam01979 1 IVLPGLIDAHVHlemgllrgIPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALLEAAeelplglrflGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 119 RDTAAVNVYPAAAITKGLAGEEmtEIGLLMQAGAVAFTDAHSSVHDTQ-VLRRIMTYAREFGAVVS---CETRDKYlgan 194
Cdd:pfam01979 81 LDTDGELEGRKALREKLKAGAE--FIKGMADGVVFVGLAPHGAPTFSDdELKAALEEAKKYGLPVAihaLETKGEV---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 195 gVMHEGLFASWLGLSGIPKEAELIPLERDLRIAqltrgRYHAAMISVPESVEAIERARsrgakvtcGISINNLALNEndi 274
Cdd:pfam01979 155 -EDAIAAFGGGIEHGTHLEVAESGGLLDIIKLI-----LAHGVHLSPTEANLLAEHLK--------GAGVAHCPFSN--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 275 geyrtffklyppLRPEDDRVAMADAVASGAIDIIVSshdpqdvdtkrlpfseaeDGAIG-------LETMLAAALRLHHG 347
Cdd:pfam01979 218 ------------SKLRSGRIALRKALEDGVKVGLGT------------------DGAGSgnslnmlEELRLALELQFDPE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 348 GQVSLMRLIDAMSTRPAQIFGL--NAGTLKPGAAADIALIDLDepwlvakdmllsrsKNTPFEDARFSGRAVATYVSGKL 425
Cdd:pfam01979 268 GGLSPLEALRMATINPAKALGLddKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKGKI 333
|
.
gi 499970679 426 V 426
Cdd:pfam01979 334 V 334
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
6-388 |
1.32e-05 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 47.00 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 6 VLKNVRIIDPSrNLDEVGTIIAeNGVIFAAGHKAQNQGAPDGAVIrDCTGLVATPGLVDARVHV---GEPGGEHRETIAS 82
Cdd:cd01308 3 LIKNAEVYAPE-YLGKKDILIA-GGKILAIEDQLNLPGYENVTVV-DLHGKILVPGFIDQHVHIiggGGEGGPSTRTPEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 83 ASRAAAAGGVTSIIMMPDTDPVIDDIALVeFVKKTARDTAAVNVY--------PAAAITKGLAgEEMTEIGLLMQAGAVA 154
Cdd:cd01308 80 TLSDLTTAGVTTVVGCLGTDGISRSMEDL-LAKARALEEEGITCFvytgsyevPTRTITGSIR-KDLLLIDKVIGVGEIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 155 FTDAHSSVHDTQVLRRIMTYAReFGAVVScetrdkylGANGVMHEGLFASWLGLSGIPKEAEliplERDLRIAQLTRGry 234
Cdd:cd01308 158 ISDHRSSQPTVEELARIAAEAR-VGGLLG--------GKAGIVHIHLGDGKRALSPIFELIE----ETEIPITQFLPT-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 235 HAAMiSVPESVEAIERARSRGA-KVTCGISinnlalnendigeyrTFFKLYPPLRPEDdrvAMADAVASG-AIDIIVSSH 312
Cdd:cd01308 223 HINR-TAPLFEQGVEFAKMGGTiDLTSSID---------------PQFRKEGEVRPSE---ALKRLLEQGvPLERITFSS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 313 DPQDvdtkRLPFSEAEDGAIGL-----ETMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGL-NAGTLKPGAAADIALID 386
Cdd:cd01308 284 DGNG----SLPKFDENGNLVGLgvgsvDTLLREVREAVKCGDIPLEVALRVITSNVARILKLrKKGEIQPGFDADLVILD 359
|
..
gi 499970679 387 LD 388
Cdd:cd01308 360 KD 361
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
5-74 |
1.65e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 47.00 E-value: 1.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 5 IVLKNVRIIDPSRNLDEVGTIIAENGVIFAAGHKAqnqGAPDgAVIrDCTGLVATPGLVDARVHVGEPGG 74
Cdd:PRK09061 21 LVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAA---IEGD-RTI-DATGLVVAPGFIDLHAHGQSVAA 85
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
334-428 |
2.24e-05 |
|
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: 46.36 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 334 LETMLAAAL--RLHHGGQ--VSLMRLIDAMSTRPAQIFGLN--AGTLKPGAAADIALIDLDEPWLvakdmllsrsknTPF 407
Cdd:COG0402 320 FEEMRLAALlqRLRGGDPtaLSAREALEMATLGGARALGLDdeIGSLEPGKRADLVVLDLDAPHL------------APL 387
|
90 100
....*....|....*....|....*...
gi 499970679 408 EDARF------SGRAV-ATYVSGKLVHA 428
Cdd:COG0402 388 HDPLSalvyaaDGRDVrTVWVAGRVVVR 415
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
294-428 |
5.30e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 45.17 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 294 VAMADAVASGAIDIIVSSHdpqdvdtkrLPFSeaedgaigletMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGLN-AG 372
Cdd:PRK15446 288 VSALDLAAAGLLDILSSDY---------YPAS-----------LLDAAFRLADDGGLDLPQAVALVTANPARAAGLDdRG 347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 499970679 373 TLKPGAAADIALIDLDEPwlvakdmllsrsknTPfedarfsgRAVATYVSGKLVHA 428
Cdd:PRK15446 348 EIAPGKRADLVRVRRAGG--------------LP--------VVRAVWRGGRRVFL 381
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
330-427 |
1.71e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 43.67 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 330 GAIGLETMLAAALRLHHGGqVSLMRLIDAMSTRPAQIFGL--NAGTLKPGAAADIALIDLDepwLVAKDmllsrskntpf 407
Cdd:pfam07969 380 AAVMRQTAGGGEVLGPDEE-LSLEEALALYTSGPAKALGLedRKGTLGVGKDADLVVLDDD---PLTVD----------- 444
|
90 100
....*....|....*....|
gi 499970679 408 EDARFSGRAVATYVSGKLVH 427
Cdd:pfam07969 445 PPAIADIRVRLTVVDGRVVY 464
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
6-68 |
3.75e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 42.39 E-value: 3.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499970679 6 VLKNVRIIDPSRNLDEvGTIIAENGVIFAAGhkaqnQGAPDGAVIRDCTGLVATPGLVDARVH 68
Cdd:COG1820 1 AITNARIFTGDGVLED-GALLIEDGRIAAIG-----PGAEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
334-426 |
7.33e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 41.71 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 334 LETMLAAAL--RLHH-GGQVSLMRLIDAMST-RPAQIFGLNAGTLKPGAAADIALIDLDEPWLvakdmllsRSKNTPFED 409
Cdd:PRK08393 307 LREMKLAALlhKVHNlDPTIADAETVFRMATqNGAKALGLKAGVIKEGYLADIAVIDFNRPHL--------RPINNPISH 378
|
90 100
....*....|....*....|
gi 499970679 410 ARFSGRA---VATYVSGKLV 426
Cdd:PRK08393 379 LVYSANGndvETTIVDGKIV 398
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
5-71 |
1.52e-03 |
|
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: 40.65 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499970679 5 IVLKNVRII--DPSRNLdEVGTIIAENGVIFAAGHKAQNQGAPDGAVIrDCTGLVATPGLVDARVHVGE 71
Cdd:cd01298 1 ILIRNGTIVttDPRRVL-EDGDVLVEDGRIVAVGPALPLPAYPADEVI-DAKGKVVMPGLVNTHTHLAM 67
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
20-68 |
2.88e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 39.79 E-value: 2.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 499970679 20 DEVGTIIAENGVIFAAGHKAQ-NQGAPDGAVIRDCTGLVATPGLVDARVH 68
Cdd:PRK09228 29 IEDGLLLVEDGRIVAAGPYAElRAQLPADAEVTDYRGKLILPGFIDTHIH 78
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
294-390 |
3.18e-03 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 39.57 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 294 VAMADAVASGAIDIIVSSHDPQdvdtkrlpfseaedgaigleTMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGL-NAG 372
Cdd:cd01306 237 VSARELAAHGLLDILSSDYVPA--------------------SLLHAAFRLADLGGWSLPEAVALVSANPARAVGLtDRG 296
|
90
....*....|....*...
gi 499970679 373 TLKPGAAADIALIDLDEP 390
Cdd:cd01306 297 SIAPGKRADLILVDDMDG 314
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
336-386 |
4.96e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 38.93 E-value: 4.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499970679 336 TMLAAALRLHHGGQVSLMRLIDAMSTRPAQIFGL--NAGTLKPGAAADIALID 386
Cdd:COG1820 308 TMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLddRKGSIAPGKDADLVVLD 360
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
2-68 |
7.60e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 38.37 E-value: 7.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499970679 2 SNPIVLKNVRIIDPSRnLDevgtIIAENGVIFAAGhkaQNQGAPDGAVIRDCTGLVATPGLVDARVH 68
Cdd:PRK05985 1 MTDLLFRNVRPAGGAA-VD----ILIRDGRIAAIG---PALAAPPGAEVEDGGGALALPGLVDGHIH 59
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
350-411 |
7.96e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 38.20 E-value: 7.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499970679 350 VSLMRLIDAMSTRPAQIFGLNA--GTLKPGAAADIALIDLdepwlvakdmllsRSKNTPFEDAR 411
Cdd:PRK12394 301 MALEDVINACTHTPAVLMGMAAeiGTLAPGAFADIAIFKL-------------KNRHVEFADIH 351
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
25-396 |
9.84e-03 |
|
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: 37.69 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 25 IIAENGVIFAAGhkaQNQGAPDGAVIRDCTGLVATPGLVDARVHV---GEPGGEHRETIASASraaaagGVTSIImmpDT 101
Cdd:cd01307 2 VAIENGKIAAVG---AALAAPAATQIVDAGGCYVSPGWIDLHVHVyqgGTRYGDRPDMIGVKS------GVTTVV---DA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 102 -DPVIDDIAlvEFVKKTARDtAAVNVYPAAAITK--GLAGEEMTEIGLL----MQAGAVAFTD------AHSSVHDTQVL 168
Cdd:cd01307 70 gSAGADNID--GFRYTVIER-SATRVYAFLNISRvgLVAQDELPDPDNIdedaVVAAAREYPDvivglkARASKSVVGEW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 169 R-RIMTYAREFGAVVSCEtrdkylgangVM-HEGlfaswlglSGIPKEAELIP-LERDLRIAQLTRGRYHAAMISVPESV 245
Cdd:cd01307 147 GiKPLELAKKIAKEADLP----------LMvHIG--------SPPPILDEVVPlLRRGDVLTHCFNGKPNGIVDEEGEVL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499970679 246 EAIERARSRGAKVtcgisinnlalnenDIGEYRTFFKLypplrpeddRVAMAdAVASGAIDIIVSShdpqDVDTKRLPFS 325
Cdd:cd01307 209 PLVRRARERGVIF--------------DVGHGTASFSF---------RVARA-AIAAGLLPDTISS----DIHGRNRTNG 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499970679 326 EAEDGAIGLETMLAAALRLHHggqvslmrLIDAMSTRPAQIFGL-NAGTLKPGAAADIALIDLDEPWLVAKD 396
Cdd:cd01307 261 PVYALATTLSKLLALGMPLEE--------VIEAVTANPARMLGLaEIGTLAVGYDADLTVFDLKDGRVELVD 324
|
|
| |
