|
Name |
Accession |
Description |
Interval |
E-value |
| pyrC |
PRK09357 |
dihydroorotase; Validated |
11-431 |
2.50e-173 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 491.63 E-value: 2.50e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 11 LVIRGAHVLDtAAGVDAVLDVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAAA 90
Cdd:PRK09357 3 ILIKNGRVID-PKGLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 91 AGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITRNQGGAELTEMAELASAGAAAFTDDGQPVVAPGLM 170
Cdd:PRK09357 82 AGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQDARLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 171 RRALQYGAVTRRRLALHCEEPTLSKGGQMHEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLHLLHLSARESVEAL 250
Cdd:PRK09357 162 RRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 251 SRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEVPFEAAP 330
Cdd:PRK09357 242 RWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 331 FGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGLDAPRIAVGAPANLVLLDLKASRRVSESDFRSRSANSWL 410
Cdd:PRK09357 322 FGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPF 401
|
410 420
....*....|....*....|.
gi 1125170799 411 LGQTVKGKVRLTIAAGRVAFE 431
Cdd:PRK09357 402 IGMKLKGKVVYTIVDGKIVYQ 422
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
12-432 |
1.77e-156 |
|
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: 449.54 E-value: 1.77e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 12 VIRGAHVLDtAAGVdAVLDVRVDGGTIVQLGTNLET-NAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIAsgtaaaa 90
Cdd:COG0044 1 LIKNGRVVD-PGGL-ERADVLIEDGRIAAIGPDLAApEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIEtgtraaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 91 aggycaILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITRNQGgAELTEMAELASA-----GAAAFTDDGQPVV 165
Cdd:COG0044 79 aggvttVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLG-ENLAELGALAEAgavafKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 166 APGLMRRALQYGAVTRRRLALHCEEPTLSKGGQMHEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLHLLHLSARE 245
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 246 SVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEVP 325
Cdd:COG0044 238 AVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKELP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 326 FEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGLD-APRIAVGAPANLVLLDLKASRRVSESDFRSR 404
Cdd:COG0044 318 FAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLPrKGRIAVGADADLVLFDPDAEWTVTAEDLHSK 397
|
410 420
....*....|....*....|....*...
gi 1125170799 405 SANSWLLGQTVKGKVRLTIAAGRVAFEG 432
Cdd:COG0044 398 SKNTPFEGRELTGRVVATIVRGRVVYED 425
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
51-422 |
2.45e-141 |
|
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: 408.55 E-value: 2.45e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 51 RVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAAAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGF 130
Cdd:cd01317 3 EVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 131 LAAITRNQGGAELTEMAELASAGAAAFTDDGQPVVAPGLMRRALQYGAVTRRRLALHCEEPTLSKGGQMHEGAVSAELGF 210
Cdd:cd01317 83 IGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRLGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 211 EGYPSVAESLMVERDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLR 290
Cdd:cd01317 163 PGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPPLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 291 AEEDRQALIAGLRDGTIGAVATDHAPHARHEKEVPFEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAY 370
Cdd:cd01317 243 SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKIL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1125170799 371 GLDAPRIAVGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLT 422
Cdd:cd01317 323 GLPPGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
30-431 |
9.49e-118 |
|
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: 349.82 E-value: 9.49e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 30 DVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAAAAGGYCAILAMPNTEPVVDS 109
Cdd:TIGR00857 7 DILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 110 AAVLGSLAETAQAEADVPVGFLAAITRNQGGAELTEMAE--LASAGAAAFTDDGQPVVAPGLMRRALQYGAVTRRRLALH 187
Cdd:TIGR00857 87 PETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYElkEAGAVGRMFTDDGSEVQDILSMRRALEYAAIAGVPIALH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 188 CEEPTLSKGGQMHEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPH 267
Cdd:TIGR00857 167 AEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 268 HLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEVPFEAAPFGVTGLETAFSALYTHL 347
Cdd:TIGR00857 247 HLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALPLLLQLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 348 VEpGLLKLETLLERMSAGPARAYGL-DAPRIAVGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAG 426
Cdd:TIGR00857 327 VK-GLISLKDLIRMLSINPARIFGLpDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRG 405
|
....*
gi 1125170799 427 RVAFE 431
Cdd:TIGR00857 406 KVVYE 410
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
12-419 |
2.29e-94 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 289.96 E-value: 2.29e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 12 VIRGAHVLDTAAGVDAVLDVRVDGGTIVQLGTNLE--TNAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAA 89
Cdd:PRK07369 5 LLQQVRVLDPVSNTDRIADVLIEDGKIQAIEPHIDpiPPDTQIIDASGLILGPGLVDLYSHSGEPGFEERETLASLAAAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 90 AAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITRNQGGAELTEMAELASAGAAAFTDdGQPVVAPGL 169
Cdd:PRK07369 85 AAGGFTRVAILPDTFPPLDNPATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTELAELAAAGVVGFTD-GQPLENLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 170 MRRALQYGAVTRRRLALHCEEPTLSKGGQMHEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLHLLHLSARESVEA 249
Cdd:PRK07369 164 LRRLLEYLKPLGKPVALWPCDRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTARSVEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 250 LSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEVPFEAA 329
Cdd:PRK07369 244 IAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVAFAEA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 330 PFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGLDAPRIAVGAPANLVLLDLKASRRVSESDFRSRSANSW 409
Cdd:PRK07369 324 PPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPPSLAPGQPAELILFDPQKTWTVSAQTLHSLSRNTP 403
|
410
....*....|
gi 1125170799 410 LLGQTVKGKV 419
Cdd:PRK07369 404 WLGQTLKGRV 413
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
11-431 |
5.09e-79 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 251.11 E-value: 5.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 11 LVIRGAHVLDTAAGVDAVLDVRVDGGTIVQLGTNLETNAH----RVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGT 86
Cdd:PRK09059 5 ILLANARIIDPSRGLDEIGTVLIEDGVIVAAGKGAGNQGApegaEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIASAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 87 AAAAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITRNQGGAELTEMAELASAGAAAFTDDGQPVVA 166
Cdd:PRK09059 85 RAAAAGGVTSIIMMPDTDPVIDDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEEMTEFGLLRAAGAVAFTDGRRSVAN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 167 PGLMRRALQY----GAVtrrrLALHCEEPTLSKGGQMHEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLHLLHLS 242
Cdd:PRK09059 165 TQVMRRALTYardfDAV----IVHETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 243 ARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEK 322
Cdd:PRK09059 241 CAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 323 EVPFEAAPFGVTGLETAFSALYtHLVEPGLLKLETLLERMSAGPARAYGLDAPRIAVGAPANLVLLDLKASRRVSESDFR 402
Cdd:PRK09059 321 RLPFSEAAAGAIGLETLLAAAL-RLYHNGEVPLLRLIEALSTRPAEIFGLPAGTLKPGAPADIIVIDLDEPWVVDPEDLK 399
|
410 420
....*....|....*....|....*....
gi 1125170799 403 SRSANSWLLGQTVKGKVRLTIAAGRVAFE 431
Cdd:PRK09059 400 SRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
11-432 |
1.00e-74 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 239.58 E-value: 1.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 11 LVIRGAHVLDTAAGVDAVLDVRVDGGTIVQLGTNLET-NAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAA 89
Cdd:PRK07627 3 IHIKGGRLIDPAAGTDRQADLYVAAGKIAAIGQAPAGfNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 90 AAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITRNQGGAELTEMAELASAGAAAFTDDGQPVVAPGL 169
Cdd:PRK07627 83 VAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGFSQANVPVVDTQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 170 MRRALQYGAVTRRRLALHCEEPTLSKGGQMHEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLHLLHLSARESVEA 249
Cdd:PRK07627 163 LLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 250 LSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEVPFEAA 329
Cdd:PRK07627 243 VRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLPFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 330 PFGVTGLETAFSALYTHLVEPGlLKLETLLERMSAGPARAYGLDAPRIAVGAPANLVLLDLKASRRVSESDFRSRSANSW 409
Cdd:PRK07627 323 TPGATGLELLLPLTLKWADEAK-VPLARALARITSAPARVLGLPAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTP 401
|
410 420
....*....|....*....|...
gi 1125170799 410 LLGQTVKGKVRLTIAAGRVAFEG 432
Cdd:PRK07627 402 FLGYELPGRVRATLVAGQVAFER 424
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
57-426 |
2.84e-68 |
|
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: 221.05 E-value: 2.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 57 GLVLAPAFVDPHVHLRTPGREDEETIASGTAAAAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITR 136
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 137 NQGGAELTEMAELASAGaaaFTDD--GQPVVAPGLMRRALqygAVTRRRLALHCEEPTLSKGGQM---HEGAVSAElgfe 211
Cdd:cd01318 81 SEDLEELDKAPPAGYKI---FMGDstGDLLDDEETLERIF---AEGSVLVTFHAEDEDRLRENRKelkGESAHPRI---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 212 gYPSVAESLMVERDLALAAYERQPLHLLHLSARESVEALSRAQVagvVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRA 291
Cdd:cd01318 151 -RDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKP---GVTVEVTPHHLFLDVEDYDRLGTLGKVNPPLRS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 292 EEDRQALIAGLRDGTIGAVATDHAPHARHEKEVPFEAAPFGVTGLETAFSALYThLVEPGLLKLETLLERMSAGPARAYG 371
Cdd:cd01318 227 REDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLT-LVNKGILSLSRVVRLTSHNPARIFG 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1125170799 372 LDAP-RIAVGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAG 426
Cdd:cd01318 306 IKNKgRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
58-422 |
4.68e-59 |
|
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: 196.07 E-value: 4.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 58 LVLAPAFVDPHVHLRTPG-REDEETIASGTAAAAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITR 136
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGgTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 137 NQGGAELTEMAELASAGAAAFTDDGQPvvapglmrralqygavtrrrlalhceEPTLSKGGQMHEGavsaelgFEGYPSV 216
Cdd:cd01302 81 GDVTDELKKLFDAGINSLKVFMNYYFG--------------------------ELFDVDDGTLMRT-------FLEIASR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 217 AESLMV--ERDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEED 294
Cdd:cd01302 128 GGPVMVhaERAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPPLRSKED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 295 RQALIAGLRDGTIGAVATDHAPHARHEKE--VPFEAAPFGVTGLETAFSALYTHLVEPGLLkLETLLERMSAGPARAYGL 372
Cdd:cd01302 208 REALWEGVKNGKIDTIASDHAPHSKEEKEsgKDIWKAPPGFPGLETRLPILLTEGVKRGLS-LETLVEILSENPARIFGL 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1125170799 373 DAP-RIAVGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLT 422
Cdd:cd01302 287 YPKgTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
10-431 |
9.84e-59 |
|
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: 198.67 E-value: 9.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 10 DLVIRGAHVLdTAAGVDAVlDVRVDGGTIVQLGTNLE-TNAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAA 88
Cdd:cd01315 1 DLVIKNGRVV-TPDGVREA-DIAVKGGKIAAIGPDIAnTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 89 AAAGGYCAILAMP-NTEPVVDSAAVLGSLAETAQAEADVPVGFLaaitrnqGGA------ELTEMAELASAGAAAFT--- 158
Cdd:cd01315 79 AAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFW-------GGLvpgnldQLRPLDEAGVVGFKCFLcps 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 159 -DDGQPVVAPGLMRRALQYGAVTRRRLALHCEEPTLSKggqmHEGAVSAELGFEGY-------PSVAESLMVERDLALAA 230
Cdd:cd01315 152 gVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITE----ALQEQAKAKGKRDYrdylasrPVFTEVEAIQRILLLAK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 231 YERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAV 310
Cdd:cd01315 228 ETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 311 ATDHAPHARHEKEVP----FEAAPfGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGLDAP--RIAVGAPAN 384
Cdd:cd01315 308 VSDHSPCTPELKLLGkgdfFKAWG-GISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQkgRIAVGYDAD 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1125170799 385 LVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAFE 431
Cdd:cd01315 387 FVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQ 433
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
9-431 |
9.44e-57 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 192.97 E-value: 9.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 9 DDLVIRGAHVLdTAAGVDAVLDVRVDGGTIVQLGTNLETNAH-RVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTA 87
Cdd:PRK07575 3 MSLLIRNARIL-LPSGELLLGDVLVEDGKIVAIAPEISATAVdTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 88 AAAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGF-LAAITRNQggAELTEMAELASAGAAAFTDDGQPVV- 165
Cdd:PRK07575 82 ACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFfIGATPDNL--PELLTANPTCGIKIFMGSSHGPLLVd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 166 APGLMRRALqygAVTRRRLALHCE-EPTLSKGGQMHEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLHLLHLSAR 244
Cdd:PRK07575 160 EEAALERIF---AEGTRLIAVHAEdQARIRARRAEFAGISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHILHLSTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 245 ESVEALSRAQVAGVvaTGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEV 324
Cdd:PRK07575 237 IEAELLRQDKPSWV--TAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIATDHAPHTLEEKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 325 PFEAAPFGVTGLETAFSALYTHLVEpGLLKLETLLERMSAGPARAYGL-DAPRIAVGAPANLVLLDLKASRRVSESDFRS 403
Cdd:PRK07575 315 PYPNSPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGIpNKGRIAPGYDADLVLVDLNTYRPVRREELLT 393
|
410 420
....*....|....*....|....*...
gi 1125170799 404 RSANSWLLGQTVKGKVRLTIAAGRVAFE 431
Cdd:PRK07575 394 KCGWSPFEGWNLTGWPVTTIVGGQIVFD 421
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
13-405 |
2.39e-56 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 192.17 E-value: 2.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 13 IRGAHVLDTAAGVDAVL---DVRVDGGTIVQLGTNLE-TNAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAA 88
Cdd:PRK02382 1 MRDALLKDGRVYYNNSLqprDVRIDGGKITAVGKDLDgSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 89 AAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITRN-QGGAELTEMAELASAGAAAFTDDGQPVVAP 167
Cdd:PRK02382 81 AAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTGNwDPLESLWERGVFALGEIFMADSTGGMGIDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 168 GLMRRALQYGAVTRRRLALHCEEPTL-SKGGQMHEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLHLLHLSARES 246
Cdd:PRK02382 161 ELFEEALAEAARLGVLATVHAEDEDLfDELAKLLKGDADADAWSAYRPAAAEAAAVERALEVASETGARIHIAHISTPEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 247 VEALSRAQVagvvaTGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEVPF 326
Cdd:PRK02382 241 VDAARREGI-----TCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAPHTREEKDADI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 327 EAAPFGVTGLETAFsALYTHLVEPGLLKLETLLERMSAGPARAYGLDAP-RIAVGAPANLVLLDLKASRRVSESDFRSRS 405
Cdd:PRK02382 316 WDAPSGVPGVETML-PLLLAAVRKNRLPLERVRDVTAANPARIFGLDGKgRIAEGYDADLVLVDPDAAREIRGDDLHSKA 394
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
10-429 |
3.07e-56 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 192.06 E-value: 3.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 10 DLVIRGAHVLdTAAGVdAVLDVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAA 89
Cdd:PRK09060 6 DLILKGGTVV-NPDGE-GRADIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 90 AAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITRNQGG--AELTEMAELASAGAAAFTDDGQPVVA- 166
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADelAELERLPGCAGIKVFMGSSTGDLLVEd 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 167 -PGLmRRALQygaVTRRRLALHCE-EPTL-SKGGQMHEGAVSAelgfegYP----SVAESLMVERDLALAAYERQPLHLL 239
Cdd:PRK09060 164 dEGL-RRILR---NGRRRAAFHSEdEYRLrERKGLRVEGDPSS------HPvwrdEEAALLATRRLVRLARETGRRIHVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 240 HLSARESVEALSRAQvagVVATGEVTPHHLCLT-DEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHA 318
Cdd:PRK09060 234 HVSTAEEIDFLADHK---DVATVEVTPHHLTLAaPECYERLGTLAQMNPPIRDARHRDGLWRGVRQGVVDVLGSDHAPHT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 319 RHEKEVPFEAAPFGVTGLETAFSALYTHlVEPGLLKLETLLERMSAGPARAYGL-DAPRIAVGAPANLVLLDLKASRRVS 397
Cdd:PRK09060 311 LEEKAKPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGIaGKGRIAVGYDADFTIVDLKRRETIT 389
|
410 420 430
....*....|....*....|....*....|..
gi 1125170799 398 ESDFRSRSANSWLLGQTVKGKVRLTIAAGRVA 429
Cdd:PRK09060 390 NEWIASRCGWTPYDGKEVTGWPVGTIVRGQRV 421
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
31-426 |
3.42e-50 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 174.51 E-value: 3.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 31 VRVDGGTIVQLGTNLetNAHRVVDGQGLVLAPAFVDPHVhlRTPGRE-DEETIASGTAAAAAGGYCAILAMPNTEPVVDS 109
Cdd:PRK08417 1 IRIKDGKITEIGSDL--KGEEILDAKGKTLLPALVDLNV--SLKNDSlSSKNLKSLENECLKGGVGSIVLYPDSTPAIDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 110 AAVLgSLAETAQAEADVPVGFLAAITRNQGG-AELTEMAELASAGAAAFTDdgqpvVAPGLMRRALQYGAVTRRRLALHC 188
Cdd:PRK08417 77 EIAL-ELINSAQRELPMQIFPSIRALDEDGKlSNIATLLKKGAKALELSSD-----LDANLLKVIAQYAKMLDVPIFCRC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 189 EEPTLSKGGQMHEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHH 268
Cdd:PRK08417 151 EDSSFDDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 269 LCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEVPFEAAPFGVTGLETAFSALYTHLV 348
Cdd:PRK08417 231 LILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYTYLV 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125170799 349 EPGLLKLETLLERMSAGPARAYGLDAPRIAVGAPANLVLLDLKASRRVSESdfrsrsaNSWLLGQTVKGKVRLTIAAG 426
Cdd:PRK08417 311 KEGIITWSELSRFTSYNPAQFLGLNSGEIEVGKEADLVLFDPNESTIIDDN-------FSLYSGDELYGKIEAVIIKG 381
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
10-430 |
9.00e-50 |
|
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: 174.88 E-value: 9.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 10 DLVIRGAHVLdTAAGVDAVlDVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAA 89
Cdd:TIGR03178 1 DLIIRGGRVI-LPNGEREA-DVGVKGGKIAAIGPDILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 90 AAGGYCAILAMP-NTEPVVDSAAVLGSLAETAQAEADVPVGFLAAIT-RNQggAELTEMAELASAGAAAF-----TDDGQ 162
Cdd:TIGR03178 79 AAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVpYNL--DDLRELDEAGVVGFKAFlspsgDDEFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 163 PVVAPGL---MRRALQYGAVtrrrLALHCEEPTLSKGGQMH---EGAVSAELGFEGYPSVAESLMVERDLALAAYERQPL 236
Cdd:TIGR03178 157 HVDDWQLykgMRELARLGQL----LLVHAENPAITSALGEEappQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 237 HLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAP 316
Cdd:TIGR03178 233 HVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 317 HARHEKEV-PFEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGLDAP-RIAVGAPANLVLLDLKASR 394
Cdd:TIGR03178 313 CTPDLKRAgDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGLAQKgRIAPGKDADFVFVDPDESY 392
|
410 420 430
....*....|....*....|....*....|....*.
gi 1125170799 395 RVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAF 430
Cdd:TIGR03178 393 TLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIY 428
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
33-432 |
1.45e-46 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 164.94 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 33 VDGGTIVQLGTNLETNAHRVVDGQGLVLaPAFVDPHVHLRTPGREDEETIASGTAAAAAGGYCAILAMPNTEPVVDSAAV 112
Cdd:PRK04250 19 IENGRISKISLRDLKGKEVIKVKGGIIL-PGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 113 LGSLAETAQ--AEADVPVGFLaaITRNQGGAEltemaelasAGAAAFTDDGQPVVAPGLMRRALQYGAVTRRR-LALHCE 189
Cdd:PRK04250 98 YEKRMRIAEkkSYADYALNFL--IAGNCEKAE---------EIKADFYKIFMGASTGGIFSENFEVDYACAPGiVSVHAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 190 EPTLSkggqmhegavsaeLGFEGYPSVAESLMVERDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVAtgEVTPHHL 269
Cdd:PRK04250 167 DPELI-------------REFPERPPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLILKSNLPWVSF--EVTPHHL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 270 CLTDEAVRsLDPNVKMNPPLRAEEDRQALIAGLRdgTIGAVATDHAPHARHEKEvpfEAAPfGVTGLETAFsALYTHLVE 349
Cdd:PRK04250 232 FLTRKDYE-RNPLLKVYPPLRSEEDRKALWENFS--KIPIIASDHAPHTLEDKE---AGAA-GIPGLETEV-PLLLDAAN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 350 PGLLKLETLLERMSAGPARAYGLDAPRIAVGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVA 429
Cdd:PRK04250 304 KGMISLFDIVEKMHDNPARIFGIKNYGIEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVV 383
|
...
gi 1125170799 430 FEG 432
Cdd:PRK04250 384 MED 386
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
10-430 |
5.91e-45 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 162.18 E-value: 5.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 10 DLVIRGAHVLdTAAGVdAVLDVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAA 89
Cdd:PRK06189 4 DLIIRGGKVV-TPEGV-YRADIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 90 AAGGYCAILAMP-NTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITrNQGGAELTEMAELASAGAAAF-----TDDGQP 163
Cdd:PRK06189 82 AAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLV-PGNLEHLRELAEAGVIGFKAFmsnsgTDEFRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 164 VVAPGL---MRRALQYGAVtrrrLALHCEEPTLSKGGQM---HEGAVSAELGFEGYPSVAESLMVERDLALAAYERQPLH 237
Cdd:PRK06189 161 SDDLTLyegMKEIAALGKI----LALHAESDALTRHLTTqarQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 238 LLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAP- 316
Cdd:PRK06189 237 FVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPc 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 317 HARHEKEVPFEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGLDAP-RIAVGAPANLVLLDLKASRR 395
Cdd:PRK06189 317 PPELKEGDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGLPQKgRLEVGADADFVLVDLDETYT 396
|
410 420 430
....*....|....*....|....*....|....*
gi 1125170799 396 VSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAF 430
Cdd:PRK06189 397 LTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVY 431
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
11-432 |
5.26e-44 |
|
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: 159.31 E-value: 5.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 11 LVIRGAHVLdTAAGVdAVLDVRVDGGTIVQLGTNLE-TNAHRVVDGQGLVLAPAFVDPHVHLRTP-----GREDEETias 84
Cdd:cd01314 1 LIIKNGTIV-TADGS-FKADILIEDGKIVAIGPNLEaPGGVEVIDATGKYVLPGGIDPHTHLELPfmgtvTADDFES--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 85 gtaaaaaggYCAILAMPNTEPVVDSAAVL--GSLAETAQ---AEADVPV----GFLAAITR--NQGGAELTEMAELASAG 153
Cdd:cd01314 76 ---------GTRAAAAGGTTTIIDFAIPNkgQSLLEAVEkwrGKADGKSvidyGFHMIITDwtDSVIEELPELVKKGISS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 154 AAAFT--------DDGQPVVApglMRRALQYGAVTrrrlALHCEEPTLSKggQMHEGAVSA-ELGFEGY----PSVAESL 220
Cdd:cd01314 147 FKVFMaykgllmvDDEELLDV---LKRAKELGALV----MVHAENGDVIA--ELQKKLLAQgKTGPEYHalsrPPEVEAE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 221 MVERDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRslDPNVK-----MNPPLRAEEDR 295
Cdd:cd01314 218 ATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW--KDWFEgakyvCSPPLRPKEDQ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 296 QALIAGLRDGTIGAVATDHAPHARHEKEV---PFEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGL 372
Cdd:cd01314 296 EALWDGLSSGTLQTVGSDHCPFNFAQKARgkdDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGL 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125170799 373 dAPR---IAVGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAFEG 432
Cdd:cd01314 376 -YPRkgtIAVGSDADLVIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVED 437
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
10-432 |
5.94e-40 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 148.40 E-value: 5.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 10 DLVIRGAHVLdTAAGvDAVLDVRVDGGTIVQLGTNletNAHRVVDGQGLVLAPAFVDPHVHLRTP-----GREDEETIAS 84
Cdd:PRK08323 2 STLIKNGTVV-TADD-TYKADVLIEDGKIAAIGAN---LGDEVIDATGKYVMPGGIDPHTHMEMPfggtvSSDDFETGTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 85 GTaaaaaggycailAMPNTEPVVDSAA------VLGSLA---ETAQAEADVPVGFLAAIT--RNQGGAELTEMAELASAG 153
Cdd:PRK08323 77 AA------------ACGGTTTIIDFALqpkgqsLREALEawhGKAAGKAVIDYGFHMIITdwNEVVLDEMPELVEEGITS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 154 AAAF--------TDDGQPVVApglMRRALQYGAVTrrrlALHCEEptlskggqmheGAVSAEL------------GFEGY 213
Cdd:PRK08323 145 FKLFmaykgalmLDDDELLRA---LQRAAELGALP----MVHAEN-----------GDAIAYLqakllaegktgpEYHAL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 214 --PSVAESLMVERDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPN-----VkMN 286
Cdd:PRK08323 207 srPPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFegakyV-MS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 287 PPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEV----PFEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERM 362
Cdd:PRK08323 286 PPLRDKEHQDALWRGLQDGDLQVVATDHCPFCFEQKKQlgrgDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELT 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125170799 363 SAGPARAYGLdAPR---IAVGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAFEG 432
Cdd:PRK08323 366 STNPAKIFGL-YPRkgtIAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVED 437
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
11-432 |
6.58e-36 |
|
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: 137.52 E-value: 6.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 11 LVIRGAHVLdTAAGVdAVLDVRVDGGTIVQLGTNLETNAH-RVVDGQGLVLAPAFVDPHVHLRTP--GREDEETIASGTA 87
Cdd:TIGR02033 1 LLIKGGTVV-NADDV-FQADVLIEGGKIVAVGDNLIPPDAvEVIDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 88 AAAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAIT---RNQGGAELTEMAELASAGAAAF-TDDGQP 163
Cdd:TIGR02033 79 AAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDIThwnDSVLEEHIPEVKEEGINSFKVFmAYKNLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 164 VVAPGL----MRRALQYGAVtrrrLALHCEeptlsKGGQMHEGAVSA-ELGFEG-------YPSVAESLMVERDLALAAY 231
Cdd:TIGR02033 159 MVDDEElfeiLKRLKELGAL----LQVHAE-----NGDIIAELQARMlAQGITGpeyhalsRPPELEAEAVARAITLAAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 232 ERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDeavRSLDPNVK------MNPPLRAEEDRQALIAGLRDG 305
Cdd:TIGR02033 230 ADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDD---THYDKPGFegakyvCSPPLREPEDQDALWSALSSG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 306 TIGAVATDHAPHARHEK-EVP---FEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGLdAPR---IA 378
Cdd:TIGR02033 307 ALQTVGSDHCTFNFAQKkAIGkddFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNL-YPRkgtIA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1125170799 379 VGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAFEG 432
Cdd:TIGR02033 386 VGSDADIVIWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVED 439
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
30-432 |
1.16e-33 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 131.15 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 30 DVRVDGGTIVQLGTNLE-TNAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAAAAGGYCAILAMPNTEPvvd 108
Cdd:PRK09236 21 DVLIENGRIAKIASSISaKSADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNP--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 109 SAAVLGSLAETAQAEADVPV---GFLAAITRNQggaeLTEMAElasagaaafTDdgqPVVAPGL---MrralqyGAVTRR 182
Cdd:PRK09236 98 PTTTLEALEAKYQIAAQRSLanySFYFGATNDN----LDEIKR---------LD---PKRVCGVkvfM------GASTGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 183 RL------------------ALHCE-EPTLSKGGQMHEGAVSAELGFEGYPSV--AE------SLMVErdlaLAAYERQP 235
Cdd:PRK09236 156 MLvdnpetlerifrdaptliATHCEdTPTIKANLAKYKEKYGDDIPAEMHPLIrsAEacykssSLAVS----LAKKHGTR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 236 LHLLHLS-AREsVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDH 314
Cdd:PRK09236 232 LHVLHIStAKE-LSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALADDRIDVIATDH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 315 APHARHEKEVPFEAAPFGVTGLETAFSALYtHLVEPGLLKLETLLERMSAGPARAYGLDApR--IAVGAPANLVLLDLKA 392
Cdd:PRK09236 311 APHTWEEKQGPYFQAPSGLPLVQHALPALL-ELVHEGKLSLEKVVEKTSHAPAILFDIKE-RgfIREGYWADLVLVDLNS 388
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1125170799 393 SRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAFEG 432
Cdd:PRK09236 389 PWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHN 428
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
10-431 |
3.28e-30 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 121.50 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 10 DLVIR-GAHVLDTAAgvdAVLDVRVDGGTIVQLGTNLETnAHRVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAA 88
Cdd:PRK08044 4 DLIIKnGTVILENEA---RVVDIAVKGGKIAAIGQDLGD-AKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 89 AAAGGYCAILAMP-NTEP-VVDSaavlgslaETAQAEADVPVGFLAAITRNQGG------AELTEMAELASAGAAAFT-- 158
Cdd:PRK08044 80 AAKGGITTMIEMPlNQLPaTVDR--------ASIELKFDAAKGKLTIDAAQLGGlvsynlDRLHELDEVGVVGFKCFVat 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 159 -------DDGQPVVAPGLMRRALQYGAvTRRRLALHCEE-PTLSKGGQM--HEGAVSAELGFEGYPSVAESLMVERDLAL 228
Cdd:PRK08044 152 cgdrgidNDFRDVNDWQFYKGAQKLGE-LGQPVLVHCENaLICDELGEEakREGRVTAHDYVASRPVFTEVEAIRRVLYL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 229 AAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIG 308
Cdd:PRK08044 231 AKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEID 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 309 AVATDHAPHARHEKEVPFEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGLDAP-RIAVGAPANLVL 387
Cdd:PRK08044 311 CLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKgRIAPGKDADFVF 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1125170799 388 LDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAFE 431
Cdd:PRK08044 391 IQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
|
|
| PLN02795 |
PLN02795 |
allantoinase |
31-431 |
5.52e-30 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 121.42 E-value: 5.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 31 VRVDGGTIVQLGTnlETNAH------RVVDGQGLVLAPAFVDPHVHLRTPGREDEETIASGTAAAAAGGYCAILAMP-NT 103
Cdd:PLN02795 64 VEVEGGRIVSVTK--EEEAPksqkkpHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 104 EPVVDSAAVLGSLAETAQAEADVPVGFLAA-ITRNQGGA-ELTEMAELASAGAAAFTD----DGQPVVAPGLMRRALQYG 177
Cdd:PLN02795 142 FPSTTSVETLELKIEAAKGKLYVDVGFWGGlVPENAHNAsVLEELLDAGALGLKSFMCpsgiNDFPMTTATHIKAALPVL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 178 AVTRRRLALHCEEPTLskgGQMHEGAVSAELGFEGY-----PS-----VAESLMVERDLALA-AYERQPLHLLHLS-ARE 245
Cdd:PLN02795 222 AKYGRPLLVHAEVVSP---VESDSRLDADPRSYSTYlksrpPSweqeaIRQLLEVAKDTRPGgVAEGAHVHIVHLSdAES 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 246 SVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARHEKEVP 325
Cdd:PLN02795 299 SLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 326 ---FEAAPFGVTGLETAFSALYTHLVEPGlLKLETLLERMSAGPARAYGLDAP-RIAVGAPANLVLLDLKASRRVSES-- 399
Cdd:PLN02795 379 egnFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGLDSKgAIAPGKDADIVVWDPEAEFVLDESyp 457
|
410 420 430
....*....|....*....|....*....|...
gi 1125170799 400 -DFRSRSANSWlLGQTVKGKVRLTIAAGRVAFE 431
Cdd:PLN02795 458 iYHKHKSLSPY-LGTKLSGKVIATFVRGNLVFL 489
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
56-432 |
3.72e-29 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 117.55 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 56 QGLVLAPAFVDPHVHLRTPGREDEETIASGTAAAAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAIT 135
Cdd:PRK00369 41 QGTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYSGVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 136 RnqggaELTEMAELASAGAAAFTDDgqpvvapgLMRRALQYGAVTRRRLA-LHCEEPTLSKGGQMHEGAVSAELGfegyp 214
Cdd:PRK00369 121 K-----DPEKVDKLPIAGYKIFPED--------LEREETFRVLLKSRKLKiLHPEVPLALKSNRKLRRNCWYEIA----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 215 svaeSLMVERDLalaayerQPLHLLHLSARESVEAlsrAQVAGvvATGEVTPHHLCLTDEAvrslDPNVKMNPPLRAEED 294
Cdd:PRK00369 183 ----ALYYVKDY-------QNVHITHASNPRTVRL---AKELG--FTVDITPHHLLVNGEK----DCLTKVNPPIRDINE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 295 RQALIAGLRDgtIGAVATDHAPHARHEKEVPFEAAPFGVTGLETAFSALYThLVEPGLLKLETLLERMSAGPARAYGLDA 374
Cdd:PRK00369 243 RLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIYT-LVSKGILSIDRAVELISTNPARILGIPY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1125170799 375 PRIAVGAPANLVLLDLKASRRVSESdfrSRSANSWLLGQTVKGKVRLTIAAGRVAFEG 432
Cdd:PRK00369 320 GEIKEGYRANFTVIQFEDWRYSTKY---SKVIETPLDGFELKASVYATIVQGKLAYLE 374
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
11-431 |
2.28e-28 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 116.48 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 11 LVIRGAHVLDtaAGVDAVLDVRVDGGTIVQLGTNLE-TNAHRVVDGQGLVLAPAFVDPHVHLRTP--GREDEETIASGTA 87
Cdd:PLN02942 7 ILIKGGTVVN--AHHQELADVYVEDGIIVAVAPNLKvPDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 88 AAaaggycaiLAMPNTEPVVDSAAVLGSLAETAQA------EADVPVGFLAAITR--NQGGAELTEMAELASAGAAAF-- 157
Cdd:PLN02942 85 AA--------LAGGTTMHIDFVIPVNGNLLAGYEAyekkaeKSCMDYGFHMAITKwdDTVSRDMETLVKEKGINSFKFfm 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 158 --------TDDgqpVVAPGLmRRALQYGAVTRrrlaLHCEEPTLSKGGQ--MHEGAVSaelGFEGY----PSVAESLMVE 223
Cdd:PLN02942 157 aykgslmvTDE---LLLEGF-KRCKSLGALAM----VHAENGDAVFEGQkrMIELGIT---GPEGHalsrPPLLEGEATA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 224 RDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRslDPNVK------MNPPLRAEEDRQA 297
Cdd:PLN02942 226 RAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLW--DPDFTiaskyvMSPPIRPAGHGKA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 298 LIAGLRDGTIGAVATDHAPHARHEKEV---PFEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGPARAYGLdA 374
Cdd:PLN02942 304 LQAALSSGILQLVGTDHCPFNSTQKAFgkdDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNI-Y 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 375 PR---IAVGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAFE 431
Cdd:PLN02942 383 PRkgaILAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWE 442
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
10-432 |
1.16e-25 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 108.63 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 10 DLVIRGAHVLdTAAGVDAVlDVRVDGGTIVQLGTNLETNAhRVVDGQGLVLAPAFVDPHVHLrtpgreDEETIASGTAAA 89
Cdd:PRK13404 5 DLVIRGGTVV-TATDTFQA-DIGIRGGRIAALGEGLGPGA-REIDATGRLVLPGGVDSHCHI------DQPSGDGIMMAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 90 AAGGYCAILAMPNTEPVVDSAA---------VLGSLAETAQAEADVPVGF---LAAITRNQGGAELTEMAELASAGAAAF 157
Cdd:PRK13404 76 DFYTGTVSAAFGGTTTVIPFAAqhrgqslreAVEDYHRRAAGKAVIDYAFhliVADPTEEVLTEELPALIAQGYTSFKVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 158 -TDDGQPVVApglmRRALQYGAVTRRRLAL---HCEeptlskggqmHEGAVS---AELGFEGY----------PSVAESL 220
Cdd:PRK13404 156 mTYDDLKLDD----RQILDVLAVARRHGAMvmvHAE----------NHDMIAwltKRLLAAGLtapkyhaisrPMLAERE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 221 MVERDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEavrSLD-PNVK-----MNPPLRAEED 294
Cdd:PRK13404 222 ATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAE---DLDrPGMEgakyiCSPPPRDKAN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 295 RQALIAGLRDGTIGAVATDHAPHA--------RHEKEVPFEAAPFGVTGLETAFSALYTHLVEPGLLKLETLLERMSAGP 366
Cdd:PRK13404 299 QEAIWNGLADGTFEVFSSDHAPFRfddtdgklAAGANPSFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNP 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125170799 367 ARAYGLdAPR---IAVGAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAFEG 432
Cdd:PRK13404 379 AKLYGL-YPRkgaIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVED 446
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
29-404 |
6.15e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 105.71 E-value: 6.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 29 LDVRVDGGTIVQLGTNLETNAHRVVDGqgLVLaPAFVDPHVHLRTPGREDEETIASGTAAAAAGGYCAILAMPNTEPVVD 108
Cdd:PRK01211 16 LEIEVEDGKIKSIKKDAGNIGKKELKG--AIL-PAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 109 SAAV----LGSLAETAQAE---------------ADVPVGFLAAI--TRNQGGAELTEmaelasAGAAAFTDDGQPVVAP 167
Cdd:PRK01211 93 DYNAfsdkLGRVAPKAYVDfslysmetgnnalilDERSIGLKVYMggTTNTNGTDIEG------GEIKKINEANIPVFFH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 168 GLMRRALQYGAVTRRRLALHceepTLSKggqmhegAVSAELGFEGYpsvaeslmverdlaLAAYERQPLHLLHLSARESV 247
Cdd:PRK01211 167 AELSECLRKHQFESKNLRDH----DLAR-------PIECEIKAVKY--------------VKNLDLKTKIIAHVSSIDVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 248 EALSRaqvagvvatgEVTPHHLCLTDEAvrSLDPNVKMNPPLRAEEDRQALIAGLRDGTIGAVATDHAPHARhEKEVPFE 327
Cdd:PRK01211 222 GRFLR----------EVTPHHLLLNDDM--PLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTE-EDKQEFE 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125170799 328 AAPFGVTGLETaFSALYTHLVEPGLLKLETLLERMSAGPARAYGLDAPRIAVGAPANLVLLDLKASRRVSESDFRSR 404
Cdd:PRK01211 289 YAKSGIIGVET-RVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKGKIEEGYDADFMAFDFTNIKKINDKRLHSK 364
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
58-430 |
9.11e-21 |
|
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: 92.90 E-value: 9.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 58 LVLAPAFVDPHVHLRTPGREDEETIASGTAAAAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGFLAAITRN 137
Cdd:cd01316 2 TIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 138 QGgAELTEmaelasagaaaFTDDgqpvvAPGLmrralqygavtrrrLALHCEepTLSKGGQMHEGAVsAELgFEGYPSV- 216
Cdd:cd01316 82 NA-ATVGE-----------LASE-----AVGL--------------KFYLNE--TFSTLILDKITAW-ASH-FNAWPSTk 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 217 -----AESLMVERDLALAAYERQPLHLLHLSARESVEALSRAQVAGVVATGEVTPHHLCLTDEAVRSLDPNVKmnPPLRA 291
Cdd:cd01316 127 pivthAKSQTLAAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQYEVR--PFLPT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 292 EEDRQALIAGLrdGTIGAVATDHAPHARHEKEVpfEAAPFGVTGLETAFSALYThLVEPGLLKLETLLERMSAGPARAYG 371
Cdd:cd01316 205 REDQEALWENL--DYIDCFATDHAPHTLAEKTG--NKPPPGFPGVETSLPLLLT-AVHEGRLTIEDIVDRLHTNPKRIFN 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1125170799 372 LDApriavgAPANLVLLDLKASRRVSESDFRSRSANSWLLGQTVKGKVRLTIAAGRVAF 430
Cdd:cd01316 280 LPP------QSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAF 332
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
10-70 |
1.71e-13 |
|
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: 71.56 E-value: 1.71e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125170799 10 DLVIRGAHVLDTAAGVDAVLDVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVH 70
Cdd:cd01297 1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTH 61
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
11-70 |
3.17e-12 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 67.57 E-value: 3.17e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125170799 11 LVIRGAHVLDTAAGVDAVLDVRVDGGTIVQLGTNLE-TNAHRVVDGQGLVLAPAFVDPHVH 70
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDgSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
59-428 |
1.49e-11 |
|
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: 65.22 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 59 VLAPAFVDPHVHLR--------TPGREDEETIASGTAAAAAGGYCAILAMPNTEPVVDSAAVLGSLAETAQAEADVPVGF 130
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALLEAAEELPLGLRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 131 LAAITRNQGGAELTEMAELASAGAAAFTDD---------GQPVVAPGLMRRALQYGAVTRRRLALHCEEptLSKGGQMHE 201
Cdd:pfam01979 81 LDTDGELEGRKALREKLKAGAEFIKGMADGvvfvglaphGAPTFSDDELKAALEEAKKYGLPVAIHALE--TKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 202 GAVSAELGFEGYPSVAESLMVERDLALAAYerqplHLLHLSARESVEALSRAQVAGVVatgevtphHLCLTDEAVRSldp 281
Cdd:pfam01979 159 AAFGGGIEHGTHLEVAESGGLLDIIKLILA-----HGVHLSPTEANLLAEHLKGAGVA--------HCPFSNSKLRS--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 282 nvkmnpplraeeDRQALIAGLRDGTIGAVATDHAPHARHekevpfeaapfGVTGLETAFSALyTHLVEPGLLKLETLLER 361
Cdd:pfam01979 223 ------------GRIALRKALEDGVKVGLGTDGAGSGNS-----------LNMLEELRLALE-LQFDPEGGLSPLEALRM 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125170799 362 MSAGPARAYGLDAP--RIAVGAPANLVLLDLKasrrvsesdfrsrsANSWLLGQTVKGKVRLTIAAGRV 428
Cdd:pfam01979 279 ATINPAKALGLDDKvgSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
10-75 |
3.82e-11 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 64.72 E-value: 3.82e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125170799 10 DLVIRGAHVLDTAAGVDAVLDVRVDGGTIVQLGTNLeTNAHRVVDGQGLVLAPAFVDPHVHLRTPG 75
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAA-IEGDRTIDATGLVVAPGFIDLHAHGQSVA 84
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
240-364 |
1.16e-10 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 62.69 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 240 HLSARESVEALSRAQvAGVVATgeVTPHHLCLT--DEAVRSLDPNVKMNPPLRAEEDRQALIAGLRDGT----IGavaTD 313
Cdd:cd01294 169 HITTADAVEYVKSCN-ENVAAT--ITPHHLLLTrdDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHpkffLG---SD 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1125170799 314 HAPHARHEKEVPFEAApfGVtgletaFSALYThlvepgLLKLETLLERMSA 364
Cdd:cd01294 243 SAPHPKSNKESSCGCA--GI------FSAPIA------LPYLAEVFEEHNA 279
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
10-71 |
5.19e-09 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 57.72 E-value: 5.19e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125170799 10 DLVIRGAHVLDTAAGVDavldVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVHL 71
Cdd:PRK07572 3 DLIVRNANLPDGRTGID----IGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
9-389 |
3.62e-08 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 54.97 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 9 DDLVIRGAHVLD-TAAGVDAVLDVRVDGGTIVQLGTNLETNAH---RVVDGQGLVLAPAFVDPHVHL---RTPGREDEET 81
Cdd:COG1228 8 GTLLITNATLVDgTGGGVIENGTVLVEDGKIAAVGPAADLAVPagaEVIDATGKTVLPGLIDAHTHLglgGGRAVEFEAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 82 IASGTAAAAAGGYCAIL-----------------AMPNTEPVVD--SAAVLGSLAETAQAEADVPVGFlAAITRNQGGAE 142
Cdd:COG1228 88 GGITPTVDLVNPADKRLrralaagvttvrdlpggPLGLRDAIIAgeSKLLPGPRVLAAGPALSLTGGA-HARGPEEARAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 143 LTEMAELASAGAAAFTDDGQPVVAPGLMRRALQYGAVTRRRLALHCeeptlskggqmhEGAVSAELGFE-GYPSVAeslm 221
Cdd:COG1228 167 LRELLAEGADYIKVFAEGGAPDFSLEELRAILEAAHALGLPVAAHA------------HQADDIRLAVEaGVDSIE---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 222 verdlalaayerqplHLLHLSArESVEALSRAQVAGVVATgevtphhlCLTDEAVRSLDPNVKMNPPLRAEEDRQALIAG 301
Cdd:COG1228 231 ---------------HGTYLDD-EVADLLAEAGTVVLVPT--------LSLFLALLEGAAAPVAAKARKVREAALANARR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 302 LRD--GTIgAVATDHAPHARHEKEVPFEAApfgvtgletafsalytHLVEPGLLKLETLleRMS-AGPARAYGLDAP--R 376
Cdd:COG1228 287 LHDagVPV-ALGTDAGVGVPPGRSLHRELA----------------LAVEAGLTPEEAL--RAAtINAAKALGLDDDvgS 347
|
410
....*....|...
gi 1125170799 377 IAVGAPANLVLLD 389
Cdd:COG1228 348 LEPGKLADLVLLD 360
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
10-70 |
7.18e-08 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 54.72 E-value: 7.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125170799 10 DLVIRGAHVLDTAAG--VDAvlDVRVDGGTIVQLGtNLETNAHRVVDGQGLVLAPAFVDPHVH 70
Cdd:COG1001 6 DLVIKNGRLVNVFTGeiLEG--DIAIAGGRIAGVG-DYIGEATEVIDAAGRYLVPGFIDGHVH 65
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
240-376 |
2.30e-07 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 52.45 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 240 HLSARESVEALSRAQVAGVVATgeVTPHHLCLTDEA--VRSLDPNVKMNPPLRAEEDRQALIAGLRDGT----IGavaTD 313
Cdd:PLN02599 193 HITTMDAVEFVESCGDGNVAAT--VTPQHLLLNRNAlfQGGLQPHNYCLPVLKREIHREALVKAATSGSkkffLG---TD 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125170799 314 HAPHARHEKEvpfeaAPFGVTGLETAFSAL--YTHLVEP--GLLKLETLlerMSAGPARAYGLdaPR 376
Cdd:PLN02599 268 SAPHPKRAKE-----ASCGCAGIYSAPVALslYAKAFEEagALDKLEAF---TSFNGPDFYGL--PR 324
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
10-71 |
3.61e-07 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 52.11 E-value: 3.61e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 10 DLVIRGAHVL---DTAAGVDAVLdvrVDGGTIVQLGTN-----LETNAHRVVDGQGLVLAPAFVDPHVHL 71
Cdd:COG1574 9 DLLLTNGRIYtmdPAQPVAEAVA---VRDGRIVAVGSDaevraLAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
10-71 |
7.25e-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: 50.98 E-value: 7.25e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125170799 10 DLVIRGAHVL--DTAAGVDAVLDVRVDGGTIVQLGTNLETNAH----RVVDGQGLVLAPAFVDPHVHL 71
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDGAVLVEDGRIAAVGPGAELPARypaaEVIDAGGKLVLPGLVNTHTHL 68
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
12-71 |
1.42e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 46.92 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125170799 12 VIRGAHVL--DTAAGVDAVLDVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVHL 71
Cdd:PRK08204 5 LIRGGTVLtmDPAIGDLPRGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRHT 66
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
13-71 |
1.54e-05 |
|
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: 46.86 E-value: 1.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 13 IRGAHVldtAAGVDAVLDVRVDGGTIVQLGTNLETNAHR-VVDGQGLVLAPAFVDPHVHL 71
Cdd:cd01293 2 LRNARL---ADGGTALVDIAIEDGRIAAIGPALAVPPDAeEVDAKGRLVLPAFVDPHIHL 58
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
10-71 |
2.27e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 46.28 E-value: 2.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125170799 10 DLVIRGAHVLDTAAGVDAVLDVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVHL 71
Cdd:PRK06038 3 DIIIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTHA 64
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
12-70 |
3.73e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 45.48 E-value: 3.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1125170799 12 VIRGAHVLdTAAGVDAVLDVRVDGGTIVQLGTNLETNAhRVVDGQGLVLAPAFVDPHVH 70
Cdd:COG1820 1 AITNARIF-TGDGVLEDGALLIEDGRIAAIGPGAEPDA-EVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
9-71 |
1.33e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 43.77 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125170799 9 DDLVIRGAHVLDTAAgvdavLDVRVDGGTIVQLGTNLETNAHR-VVDGQGLVLAPAFVDPHVHL 71
Cdd:PRK05985 2 TDLLFRNVRPAGGAA-----VDILIRDGRIAAIGPALAAPPGAeVEDGGGALALPGLVDGHIHL 60
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
11-71 |
1.97e-04 |
|
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: 43.34 E-value: 1.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125170799 11 LVIRGAHVLDT-AAGVDAVLDVRVDGGTIVQLGTNLETNAH---RVVDGQGLVLAPAFVDPHVHL 71
Cdd:cd01298 1 ILIRNGTIVTTdPRRVLEDGDVLVEDGRIVAVGPALPLPAYpadEVIDAKGKVVMPGLVNTHTHL 65
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
11-70 |
3.98e-04 |
|
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: 42.18 E-value: 3.98e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125170799 11 LVIRGAHVLDtaAGVDAVLDVRVDGGTIVQLGTNLE-TNAHRVVDGQGLVLAPAFVDPHVH 70
Cdd:cd00854 1 LIIKNARILT--PGGLEDGAVLVEDGKIVAIGPEDElEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
336-432 |
1.69e-03 |
|
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: 40.58 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125170799 336 LETAFSALYTHLV---EPGLLKLETLLERMSAGPARAYGLDAP--RIAVGAPANLVLLDLKASRRVSESDfrsrsANSWL 410
Cdd:COG0402 320 FEEMRLAALLQRLrggDPTALSAREALEMATLGGARALGLDDEigSLEPGKRADLVVLDLDAPHLAPLHD-----PLSAL 394
|
90 100
....*....|....*....|..
gi 1125170799 411 LGQTVKGKVRLTIAAGRVAFEG 432
Cdd:COG0402 395 VYAADGRDVRTVWVAGRVVVRD 416
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
33-71 |
2.70e-03 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 39.98 E-value: 2.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1125170799 33 VDGGTIVQLGTNLETNAH-----RVVDGQGLVLAPAFVDPHVHL 71
Cdd:cd01300 4 VRDGRIVAVGSDAEAKALkgpatEVIDLKGKTVLPGFIDSHSHL 47
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
36-71 |
5.35e-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: 38.83 E-value: 5.35e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1125170799 36 GTIVQLGTNLETNAH-RVVDGQGLVLAPAFVDPHVHL 71
Cdd:cd01309 2 GKIVAVGAEITTPADaEVIDAKGKHVTPGLIDAHSHL 38
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
11-70 |
6.94e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 38.63 E-value: 6.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125170799 11 LVIRGAHVL--DTAAGVDAvlDVRVDGGTIVQLGTNLETNAHRVVDGQGLVLAPAFVDPHVH 70
Cdd:PRK08393 3 ILIKNGYVIygENLKVIRA--DVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTH 62
|
|
| |
